| Version |
2.5 |
| Creation Date |
2005-11-16 15:48:42 |
| Update Date |
2009-05-05 20:57:48 |
| Accession Number |
HMDB00247 |
| Secondary Accession Numbers |
Not Available |
| Common Name |
Sorbitol |
| Description |
A polyhydric alcohol with about half the sweetness of sucrose. Sorbitol occurs naturally and is also produced synthetically from glucose. It was formerly used as a diuretic and may still be used as a laxative and in irrigating solutions for some surgical procedures. It is also used in many manufacturing processes, as a pharmaceutical aid, and in several research applications. Ascorbic acid fermentation; in solution form for moisture-conditioning of cosmetic creams and lotions, toothpaste, tobacco, gelatin; bodying agent for paper, textiles, and liquid pharmaceuticals; softener for candy; sugar crystallization inhibitor; surfactants; urethane resins and rigid foams; plasticizer, stabilizer for vinyl resins; food additive (sweetener, humectant, emulsifier, thickener, anticaking agent); dietary supplement. (Hawley's Condensed Chemical Dictionary) Biological Source: Occurs widely in plants ranging from algae to the higher orders. Fruits of the plant family Rosaceae, which include apples, pears, cherries, apricots, contain appreciable amounts. Rich sources are the fruits of the Sorbus and Crataegus spp. Use/Importance: Used for manuf. of sorbose, propylene glycol, ascorbic acid, resins, plasticizers and as antifreeze mixtures with glycerol or glycol. Tablet diluent, sweetening agent and humectant, other food uses. Used in photometric determination of Ru(VI) and Ru(VIII); in acid-base titration of borate (Dictionary of Organic Compounds) |
| Synonyms |
- (-)-Sorbitol
- Cystosol
- D-Glucitol
- D-Sorbitol
- D-Sorbol
- Diakarmon
- Esasorb
- Foodol D 70
- Glucarine
- Glucitol
- Karion
- Karion instant
- Kyowa Powder 50M
- L-Gulitol
- Multitol
- Neosorb
- Neosorb 20/60DC
- Neosorb 70/02
- Neosorb 70/70
- Neosorb P 20/60
- Neosorb P 60
- Neosorb P 60W
- Nivitin
- Resulax
- Sionit
- Sionit K
- Sionite
- Sionon
- Siosan
- Sorbex M
- Sorbex R
- Sorbex Rp
- Sorbex S
- Sorbex X
- Sorbilande
- Sorbilax
- Sorbit
- Sorbit D 70
- Sorbit D-Powder
- Sorbit DP
- Sorbit DP 50
- Sorbit Kyowa Powder 50M
- Sorbit L 70
- Sorbit S
- Sorbit T 70
- Sorbit W 70
- Sorbit W-Powder
- Sorbit W-Powder 50
- Sorbit WP
- Sorbite
- Sorbitol F
- Sorbitol FK
- Sorbitol FP
- Sorbitol S
- Sorbitol syrup C
- Sorbitur
- Sorbo
- Sorbogem 712
- Sorbol
- Sorbostyl
|
| Chemical IUPAC Name |
(2R,3R,4R,5S)-1,2,3,4,5,6-hexanol |
| Chemical Formula |
C6H14O6 |
| Chemical Structure |
 |
| Chemical Taxonomy |
| Kingdom |
|
| Super Class |
|
| Class |
|
| Sub Class |
|
| Family |
|
| Species |
- primary alcohol
- secondary alcohol
- 1,2-diol
|
| Biofunction |
- Component of Fructose and mannose metabolism
|
| Application |
| — |
| Source |
|
|
| Average Molecular Weight |
182.172 |
| Monoisotopic Molecular Weight |
182.079041 |
| Isomeric SMILES |
OC[C@H](O)[C@@H](O)[C@H](O)[C@H](O)CO |
| Canonical SMILES |
OCC(O)C(O)C(O)C(O)CO |
| KEGG Compound ID |
C00794  |
| BioCyc ID |
Not Available |
| BiGG ID |
36018  |
| Wikipedia Link |
Sorbitol  |
| NuGOwiki Link |
HMDB00247  |
| Metagene Link |
HMDB00247  |
| METLIN ID |
143  |
| PubChem Compound |
5780  |
| PubChem Substance |
820002  |
| ChEBI ID |
Not Available |
| CAS Registry Number |
50-70-4 |
| InChI Identifier |
InChI=1/C6H14O6/c7-1-3(9)5(11)6(12)4(10)2-8/h3-12H,1-2H2/t3-,4+,5-,6-/m1/s1 |
| Synthesis Reference |
Liu, Haichao; Luo, Chen. Method for manufacturing sorbitol and mannitol with cellulose. Faming Zhuanli Shenqing Gongkai Shuomingshu (2007), 8pp. |
| Melting Point (Experimental) |
11 oC |
| Experimental Water Solubility |
2750.0 mg/mL [MULLIN,JW (1972)]
Source: PhysProp
|
| Predicted Water Solubility |
229.0 mg/mL [Predicted by ALOGPS]
Calculated using ALOGPS
|
| Physiological Charge |
0 |
| State |
Liquid |
| Experimental LogP/Hydrophobicity |
-2.20 [SANGSTER (1994)]
Source: PhysProp
|
| Predicted LogP/Hydrophobicity |
-2.68 [Predicted by ALOGPS]; -3.9 [Predicted by PubChem via XLOGP]
Calculated using ALOGPS
|
| Material Safety Data Sheet (MSDS) |
|
| MOL File |
Show |
| SDF File |
Show |
| PDB File |
Show |
| 2D Structure |
|
| 3D Structure |
|
| Experimental PDB ID |
1D8C  |
| Experimental PDB File |
Show |
| Experimental PDB Structure |
|
| Experimental 1H NMR Spectrum |
Download Spectrum Download FID (Varian) Show Experimental Conditions  |
| Experimental 13C NMR Spectrum |
Download Spectrum Download FID (Bruker) Show Experimental Conditions  |
| Experimental 13C HSQC Spectrum |
Download Spectrum Download FID (Bruker) Show Experimental Conditions  |
| Predicted 1H NMR Spectrum |
Show Image Show Peaklist
|
| Predicted 13C NMR Spectrum |
Show Image Show Peaklist
|
| Mass Spectrum |
|
| Simplified TOCSY Spectrum |
Not Available |
| BMRB Spectrum |
Not Available |
| Cellular Location |
- Cytoplasm (Predicted from LogP)
|
| Biofluid Location |
- Blood
- Cerebrospinal Fluid
- Saliva
- Urine
|
| Tissue Location |
| Tissue |
References |
| Adipose Tissue |
— |
| Adrenal Medulla |
— |
| Bladder |
— |
| Erythrocyte |
— |
| Eye Lens |
— |
| Fibroblasts |
— |
| Kidney |
— |
| Lens |
— |
| Liver |
— |
| Nerve Cells |
— |
| Neuron |
— |
| Placenta |
— |
| Platelet |
— |
| Red Blood Cell |
— |
| Retina |
— |
| Sciatic Nerve |
— |
|
| Concentrations (Normal) |
| Biofluid |
Blood |
| Value |
1.09 +/- 0.37 uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Shetty HU, Holloway HW, Rapoport SI: Capillary gas chromatography combined with ion trap detection for quantitative profiling of polyols in cerebrospinal fluid and plasma. Anal Biochem. 1995 Jan 1;224(1):279-85. [PubMed
]
|
| Biofluid |
Blood |
| Value |
13.0 (4.0-24.0) uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
|
| Biofluid |
CSF |
| Value |
15.6 +/- 1.9 uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Regenold WT, Kling MA, Hauser P: Elevated sorbitol concentration in the cerebrospinal fluid of patients with mood disorders. Psychoneuroendocrinology. 2000 Aug;25(6):593-606. [PubMed
]
|
| Biofluid |
CSF |
| Value |
17.2 +/- 4.6 uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
|
| Biofluid |
CSF |
| Value |
13.0 (9.49-16.5) uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Shetty HU, Holloway HW, Rapoport SI: Capillary gas chromatography combined with ion trap detection for quantitative profiling of polyols in cerebrospinal fluid and plasma. Anal Biochem. 1995 Jan 1;224(1):279-85. [PubMed
]
|
| Biofluid |
CSF |
| Value |
19.43 +/- 5.65 uM |
| Age |
Adult:>18 yrs old |
| Sex |
N/A |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Shetty HU, Holloway HW, Schapiro MB: Cerebrospinal fluid and plasma distribution of myo-inositol and other polyols in Alzheimer disease. Clin Chem. 1996 Feb;42(2):298-302. [PubMed
]
|
| Biofluid |
CSF |
| Value |
19.4 +/- 5.6 uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Shetty HU, Holloway HW, Schapiro MB: Cerebrospinal fluid and plasma distribution of myo-inositol and other polyols in Alzheimer disease. Clin Chem. 1996 Feb;42(2):298-302. [PubMed
]
|
| Biofluid |
Saliva |
| Value |
<1.00 uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Morenkova SA: [Comparative analysis of dependence of saliva sorbitol and fructosamine levels on blood glucose level in patients with diabetes] Biomed Khim. 2004;50(6):612-4. [PubMed
]
|
| Biofluid |
Urine |
| Value |
3.5 +/- 2.24 umol/mmol creatinine |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Geigy Scientific Tables, 8th Rev edition, pp. 130. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
|
| Biofluid |
Urine |
| Value |
9.74 +/- 10.36 umol/mmol creatinine |
| Age |
Infant:0-1 yr old |
| Sex |
Both |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Shoemaker JD, Elliott WH: Automated screening of urine samples for carbohydrates, organic and amino acids after treatment with urease. J Chromatogr. 1991 Jan 2;562(1-2):125-38. [PubMed
]
|
|
| Concentrations (Abnormal) |
| Biofluid |
CSF |
| Value |
22.89 +/- 3.34 uM |
| Age |
N/A |
| Sex |
N/A |
| Condition |
Alzheimer's disease |
| Comments |
Not Available |
| References |
- Shetty HU, Holloway HW, Schapiro MB: Cerebrospinal fluid and plasma distribution of myo-inositol and other polyols in Alzheimer disease. Clin Chem. 1996 Feb;42(2):298-302. [PubMed
]
|
| Biofluid |
CSF |
| Value |
23.3 +/- 3.3 uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Condition |
Alzheimer's disease |
| Comments |
Not Available |
| References |
- Shetty HU, Holloway HW, Schapiro MB: Cerebrospinal fluid and plasma distribution of myo-inositol and other polyols in Alzheimer disease. Clin Chem. 1996 Feb;42(2):298-302. [PubMed
]
|
|
| Associated Disorders |
| Condition |
References |
| Alzheimer's disease |
- Shetty HU, Holloway HW, Schapiro MB: Cerebrospinal fluid and plasma distribution of myo-inositol and other polyols in Alzheimer disease. Clin Chem. 1996 Feb;42(2):298-302. [PubMed
]
|
|
| OMIM ID |
|
| Pathways |
|
| General References |
- Sundkvist G, Dahlin LB, Nilsson H, Eriksson KF, Lindgarde F, Rosen I, Lattimer SA, Sima AA, Sullivan K, Greene DA: Sorbitol and myo-inositol levels and morphology of sural nerve in relation to peripheral nerve function and clinical neuropathy in men with diabetic, impaired, and normal glucose tolerance. Diabet Med. 2000 Apr;17(4):259-68. [PubMed
]
- Morenkova SA: [Comparative analysis of dependence of saliva sorbitol and fructosamine levels on blood glucose level in patients with diabetes] Biomed Khim. 2004;50(6):612-4. [PubMed
]
- Bareford D, Jennings PE, Stone PC, Baar S, Barnett AH, Stuart J: Effects of hyperglycaemia and sorbitol accumulation on erythrocyte deformability in diabetes mellitus. J Clin Pathol. 1986 Jul;39(7):722-7. [PubMed
]
- Ciuchi E, Odetti P, Prando R: Relationship between glutathione and sorbitol concentrations in erythrocytes from diabetic patients. Metabolism. 1996 May;45(5):611-3. [PubMed
]
- Kwang-Hyok S, Ui-Nam P, Sarkar C, Bhadra R: A sensitive assay of red blood cell sorbitol level by high performance liquid chromatography: potential for diagnostic evaluation of diabetes. Clin Chim Acta. 2005 Apr;354(1-2):41-7. Epub 2005 Jan 18. [PubMed
]
- Nau R: Osmotherapy for elevated intracranial pressure: a critical reappraisal. Clin Pharmacokinet. 2000 Jan;38(1):23-40. [PubMed
]
- Belanger DR, Tierney MG, Dickinson G: Effect of sodium polystyrene sulfonate on lithium bioavailability. Ann Emerg Med. 1992 Nov;21(11):1312-5. [PubMed
]
- Ciuchi E, Odetti P, Prando R: The effect of acute glutathione treatment on sorbitol level in erythrocytes from diabetic patients. Diabetes Metab. 1997 Feb;23(1):58-60. [PubMed
]
- Shinohara R, Ohta Y, Yamauchi M, Ishiguro I: Improved fluorometric enzymatic sorbitol assay in human blood. Clin Chim Acta. 1998 May 25;273(2):171-84. [PubMed
]
- Peterson MJ, Page MG, Just LJ, Aldinger CE, Malone JI: Applicability of red blood cell sorbitol measurements to monitor the clinical activity of sorbinil. Metabolism. 1986 Apr;35(4 Suppl 1):93-5. [PubMed
]
- Vertommen J, Rillaerts E, Gysels M, De Leeuw I: Erythrocyte sorbitol content in diabetic patients: relation to metabolic control. Diabete Metab. 1987 Jun;13(3):182-6. [PubMed
]
- Cunningham JJ, Mearkle PL, Brown RG: Vitamin C: an aldose reductase inhibitor that normalizes erythrocyte sorbitol in insulin-dependent diabetes mellitus. J Am Coll Nutr. 1994 Aug;13(4):344-50. [PubMed
]
- Airey CM, Price DE, Kemp JV, Perkins CM, Wales JK: The effect of aldose reductase inhibition on erythrocyte polyols and galactitol accumulation in diabetic patients. Diabet Med. 1989 Dec;6(9):804-8. [PubMed
]
- Kamon N, Mabuchi H, Takeda R, Terashima H: Effects of aldose reductase inhibitor (ONO-2235) on human erythrocyte sorbitol concentrations in 75 g oral glucose tolerance tests. Horm Metab Res. 1991 May;23(5):226-9. [PubMed
]
- Sizeland PC, Chambers ST, Lever M, Bason LM, Robson RA: Short-term response of nonurea organic osmolytes in human kidney to a water load and water deprivation. Am J Physiol. 1995 Feb;268(2 Pt 2):F227-33. [PubMed
]
- Shetty HU, Holloway HW, Rapoport SI: Capillary gas chromatography combined with ion trap detection for quantitative profiling of polyols in cerebrospinal fluid and plasma. Anal Biochem. 1995 Jan 1;224(1):279-85. [PubMed
]
- van Griensven JM, Jusko WJ, Lemkes HH, Kroon R, Verhorst CJ, Chiang ST, Cohen AF: Tolrestat pharmacokinetic and pharmacodynamic effects on red blood cell sorbitol levels in normal volunteers and in patients with insulin-dependent diabetes. Clin Pharmacol Ther. 1995 Dec;58(6):631-40. [PubMed
]
- Regenold WT, Kling MA, Hauser P: Elevated sorbitol concentration in the cerebrospinal fluid of patients with mood disorders. Psychoneuroendocrinology. 2000 Aug;25(6):593-606. [PubMed
]
- Gehring H, Hornberger C, Dibbelt L, Dorges V, Eichenauer R, Schmucker P: Detecting and quantifying absorbed irrigation fluid by measuring mannitol and sorbitol concentrations in serum samples, and by ethanol monitoring. BJU Int. 2002 Feb;89(3):202-7. [PubMed
]
- Burggraaf J, Schoemaker RC, Lentjes EG, Cohen AF: Sorbitol as a marker for drug-induced decreases of variable duration in liver blood flow in healthy volunteers. Eur J Pharm Sci. 2000 Dec;12(2):133-9. [PubMed
]
- Wikipedia

|
| Metabolic Enzymes |
- Aldose reductase
- Glucokinase
- Hexokinase-3
- Hexokinase-2
- Sorbitol dehydrogenase
- Alpha-galactosidase A precursor
- Glycophorin B precursor
- cDNA FLJ78173, highly similar to Homo sapiens hexokinase 1 (HK1) mRNA
- cDNA, FLJ93978, Homo sapiens aldo-keto reductase family 1, member B1 (aldosereductase) (AKR1B1), mRNA (Aldo-keto reductase family 1, member B1 (Aldose reductase), isoform CRA_a)
|
|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5320 |
| Enzyme 1 Name |
Aldose reductase |
| Enzyme 1 Synonyms |
- AR
- Aldehyde reductase
|
| Enzyme 1 Gene Name |
AKR1B1 |
| Enzyme 1 Protein Sequence |
>Aldose reductase
MASRLLLNNGAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQ
EKLREQVVKREELFIVSKLWCTYHEKGLVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGK
EFFPLDESGNVVPSDTNILDTWAAMEELVDEGLVKAIGISNFNHLQVEMILNKPGLKYKP
AVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPRIKAIAAK
HNKTTAQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTLLSYNRNWRVCA
LLSCTSHKDYPFHEEF
|
| Enzyme 1 Number of Residues |
316 |
| Enzyme 1 Molecular Weight |
35854 |
| Enzyme 1 Theoretical pI |
6.99 |
| Enzyme 1 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 1 General Function |
Not Available |
| Enzyme 1 Specific Function |
Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- alditol + NAD(P)+ = aldose + NAD(P)H + H+
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
178487  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
P15121  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
ALDR_HUMAN  |
| Enzyme 1 PDB ID |
1T40  |
| Enzyme 1 PDB File |
Show |
| Enzyme 1 3D Structure |
|
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>951 bp
ATGGCAAGCCGTCTCCTGCTCAACAACGGCGCCAAGATGCCCATCCTGGGGTTGGGTACC
TGGAAGTCCCCTCCAGGGCAGGTGACTGAGGCCGTGAAGGTGGCCATTGACGTCGGGTAC
CGCCACATCGACTGTGCCCATGTGTACCAGAATGAGAATGAGGTGGGGGTGGCCATTCAG
GAGAAGCTCAGGGAGCAGGTGGTGAAGCGTGAGGAGCTCTTCATCGTCAGCAAGCTGTGG
TGCACGTACCATGAGAAGGGCCTGGTGAAAGGAGCCTGCCAGAAGACACTCAGCGACCTG
AAGCTGGACTACCTGGACCTCTACCTTATTCACTGGCCGACTGGCTTTAAGCCTGGGAAG
GAATTTTTCCCATTGGATGAGTCGGGCAATGTGGTTCCCAGTGACACCAACATTCTGGAC
ACGTGGGCGGCCATGGAAGAGCTGGTGGATGAAGGGCTGGTGAAAGCTATTGGCATCTCC
AACTTCAACCATCTCCAGGTGGAGATGATCTTAAACAAACCTGGCTTGAAGTATAAGCCT
GCAGTTAACCAGATTGAGTGCCACCCATATCTCACTCAGGAGAAGTTAATCCAGTACTGC
CAGTCCAAAGGCATCGTGGTGACCGCCTACAGCCCCCTCGGCTCTCCTGACAGGCCCTGG
GCCAAGCCCGAGGACCCTTCTCTCCTGGAGGATCCCAGGATCAAGGCGATCGCAGCCAAG
CACAATAAAACTACAGCCCAGGTCCTGATCCGGTTCCCCATGCAGAGGAACTTGGTGGTG
ATCCCCAAGTCTGTGACACCAGAACGCATTGCTGAGAACTTTAAGGTCTTTGACTTTGAA
CTGAGCAGCCAGGATATGACCACCTTACTCAGCTACAACAGGAACTGGAGGGTCTGTGCC
TTGTTGAGCTGTACCTCCCACAAGGATTACCCCTTCCATGAAGAGTTTTGA
|
| Enzyme 1 GenBank Gene ID |
J04795  |
| Enzyme 1 GeneCard ID |
AKR1B1  |
| Enzyme 1 GenAtlas ID |
AKR1B1  |
| Enzyme 1 HGNC ID |
HGNC:381  |
| Enzyme 1 Chromosome Location |
7 |
| Enzyme 1 Locus |
7q35 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Bohren KM, Bullock B, Wermuth B, Gabbay KH: The aldo-keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases. J Biol Chem. 1989 Jun 5;264(16):9547-51. [PubMed
]
- Chung S, LaMendola J: Cloning and sequence determination of human placental aldose reductase gene. J Biol Chem. 1989 Sep 5;264(25):14775-7. [PubMed
]
- Graham A, Hedge PJ, Powell SJ, Riley J, Brown L, Gammack A, Carey F, Markham AF: Nucleotide sequence of cDNA for human aldose reductase. Nucleic Acids Res. 1989 Oct 25;17(20):8368. [PubMed
]
- Grundmann U, Bohn H, Obermeier R, Amann E: Cloning and prokaryotic expression of a biologically active human placental aldose reductase. DNA Cell Biol. 1990 Apr;9(3):149-57. [PubMed
]
- Nishimura C, Matsuura Y, Kokai Y, Akera T, Carper D, Morjana N, Lyons C, Flynn TG: Cloning and expression of human aldose reductase. J Biol Chem. 1990 Jun 15;265(17):9788-92. [PubMed
]
- Graham A, Brown L, Hedge PJ, Gammack AJ, Markham AF: Structure of the human aldose reductase gene. J Biol Chem. 1991 Apr 15;266(11):6872-7. [PubMed
]
- Ko BC, Ruepp B, Bohren KM, Gabbay KH, Chung SS: Identification and characterization of multiple osmotic response sequences in the human aldose reductase gene. J Biol Chem. 1997 Jun 27;272(26):16431-7. [PubMed
]
- Ferraretto A, Negri A, Giuliani A, De Grada L, Fuhrman Conti AM, Ronchi S: Aldose reductase is involved in long-term adaptation of EUE cells to hyperosmotic stress. Biochim Biophys Acta. 1993 Feb 17;1175(3):283-8. [PubMed
]
- Morjana NA, Lyons C, Flynn TG: Aldose reductase from human psoas muscle. Affinity labeling of an active site lysine by pyridoxal 5'-phosphate and pyridoxal 5'-diphospho-5'-adenosine. J Biol Chem. 1989 Feb 15;264(5):2912-9. [PubMed
]
- Liu SQ, Bhatnagar A, Ansari NH, Srivastava SK: Identification of the reactive cysteine residue in human placenta aldose reductase. Biochim Biophys Acta. 1993 Aug 7;1164(3):268-72. [PubMed
]
- Jaquinod M, Potier N, Klarskov K, Reymann JM, Sorokine O, Kieffer S, Barth P, Andriantomanga V, Biellmann JF, Van Dorsselaer A: Sequence of pig lens aldose reductase and electrospray mass spectrometry of non-covalent and covalent complexes. Eur J Biochem. 1993 Dec 15;218(3):893-903. [PubMed
]
- Tarle I, Borhani DW, Wilson DK, Quiocho FA, Petrash JM: Probing the active site of human aldose reductase. Site-directed mutagenesis of Asp-43, Tyr-48, Lys-77, and His-110. J Biol Chem. 1993 Dec 5;268(34):25687-93. [PubMed
]
- Wilson DK, Bohren KM, Gabbay KH, Quiocho FA: An unlikely sugar substrate site in the 1.65 A structure of the human aldose reductase holoenzyme implicated in diabetic complications. Science. 1992 Jul 3;257(5066):81-4. [PubMed
]
- Borhani DW, Harter TM, Petrash JM: The crystal structure of the aldose reductase.NADPH binary complex. J Biol Chem. 1992 Dec 5;267(34):24841-7. [PubMed
]
- Wilson DK, Tarle I, Petrash JM, Quiocho FA: Refined 1.8 A structure of human aldose reductase complexed with the potent inhibitor zopolrestat. Proc Natl Acad Sci U S A. 1993 Nov 1;90(21):9847-51. [PubMed
]
- Harrison DH, Bohren KM, Petsko GA, Ringe D, Gabbay KH: The alrestatin double-decker: binding of two inhibitor molecules to human aldose reductase reveals a new specificity determinant. Biochemistry. 1997 Dec 23;36(51):16134-40. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5442 |
| Enzyme 2 Name |
Glucokinase |
| Enzyme 2 Synonyms |
- Hexokinase-4
- Hexokinase type IV
- HK IV
- HK4
- Hexokinase-D
|
| Enzyme 2 Gene Name |
GCK |
| Enzyme 2 Protein Sequence |
>Glucokinase
MLDDRARMEAAKKEKVEQILAEFQLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPT
YVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGEEGQWSVKTKHQMYSIPEDAMTGTAE
MLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNN
VVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQN
VELVEGDEGRMCVNTEWGAFGDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGE
LVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFVSQVESDTGDRKQIYNILSTLGLRPS
TTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHPSFK
ERFHASVRRLTPSCEITFIESEEGSGRGAALVSAVACKKACMLGQ
|
| Enzyme 2 Number of Residues |
465 |
| Enzyme 2 Molecular Weight |
52192 |
| Enzyme 2 Theoretical pI |
4.85 |
| Enzyme 2 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- hexokinase activity
- nucleotide binding
- phosphotransferase activity, alcohol group as acceptor
- purine nucleotide binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- alcohol metabolism
- cellular metabolism
- glucose catabolism
- glucose metabolism
- glycolysis
- hexose metabolism
- metabolism
- monosaccharide metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 2 General Function |
Not Available |
| Enzyme 2 Specific Function |
Catalyzes the initial step in utilization of glucose by the beta-cell and liver at physiological glucose concentration. Glucokinase has a high Km for glucose, and so it is effective only when glucose is abundant. The role of GCK is to provide G6P for the synthesis of glycogen. Pancreatic glucokinase plays an important role in modulating insulin secretion. Hepatic glucokinase helps to facilitate the uptake and conversion of glucose by acting as an insulin-sensitive determinant of hepatic glucose usage |
| Enzyme 2 Pathways |
|
| Enzyme 2 Reactions |
- ATP + D-glucose = ADP + D-glucose 6-phosphate
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
179427  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P35557  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
HXK4_HUMAN  |
| Enzyme 2 PDB ID |
1V4T  |
| Enzyme 2 PDB File |
Show |
| Enzyme 2 3D Structure |
|
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>1398 bp
ATGCTGGACGACAGAGCCAGGATGGAGGCCGCCAAGAAGGAGAAGGTAGAGCAGATCCTG
GCAGAGTTCCAGCTGCAGGAGGAGGACCTGAAGAAGGTGATGAGACGGATGCAGAAGGAG
ATGGACCGCGGCCTGAGGCTGGAGACCCATGAAGAGGCCAGTGTGAAGATGCTGCCCACC
TACGTGCGCTCCACCCCAGAAGGCTCAGAAGTCGGGGACTTCCTCTCCCTGGACCTGGGT
GGCACTAACTTCAGGGTGATGCTGGTGAAGGTGGGAGAAGGTGAGGAGGGGCAGTGGAGC
GTGAAGACCAAACACCAGATGTACTCCATCCCCGAGGACGCCATGACCGGCACTGCTGAG
ATGCTCTTCGACTACATCTCTGAGTGCATCTCCGACTTCCTGGACAAGCATCAGATGAAA
CACAAGAAGCTGCCCCTGGGCTTCACCTTCTCCTTTCCTGTGAGGCACGAAGACATCGAT
AAGGGCATCCTTCTCAACTGGACCAAGGGCTTCAAGGCCTCAGGAGCAGAAGGGAACAAT
GTCGTGGGGCTTCTGCGAGACGCTATCAAACGGAGAGGGGACTTTGAAATGGATGTGGTG
GCAATGGTGAATGACACGGTGGCCACGATGATCTCCTGCTACTACGAAGACCATCAGTGC
GAGGTCGGCATGATCGTGGGCACGGGCTGCAATGCCTGCTACATGGAGGAGATGCAGAAT
GTGGAGCTGGTGGAGGGGGACGAGGGCCGCATGTGCGTCAATACCGAGTGGGGCGCCTTC
GGGGACTCCGGCGAGCTGGACGAGTTCCTGCTGGAGTATGACCGCCTGGTGGACGAGAGC
TCTGCAAACCCCGGTCAGCAGCTGTATGAGAAGCTCATAGGTGGCAAGTACATGGGCGAG
CTGGTGCGGCTTGTGCTGCTCAGGCTCGTGGACGAAAACCTGCTCTTCCACGGGGAGGCC
TCCGAGCAGCTGCGCACACGCGGAGCCTTCGAGACGCGCTTCGTGTCGCAGGTGGAGAGC
GACACGGGCGACCGCAAGCAGATCTACAACATCCTGAGCACGCTGGGGCTGCGACCCTCG
ACCACCGACTGCGACATCGTGCGCCGCGCCTGCGAGAGCGTGTCTACGCGCGCTGCGCAC
ATGTGCTCGGCGGGGCTGGCGGGCGTCATCAACCGCATGCGCGAGAGCCGCAGCGAGGAC
GTAATGCGCATCACTGTGGGCGTGGATGGCTCCGTGTACAAGCTGCACCCCAGCTTCAAG
GAGCGGTTCCATGCCAGCGTGCGCAGGCTGACGCCCAGCTGCGAGATCACCTTCATCGAG
TCGGAGGAGGGCAGTGGCCGGGGCGCGGCCCTGGTCTCGGCGGTGGCCTGTAAGAAGGCC
TGTATGCTGGGCCAGTGA
|
| Enzyme 2 GenBank Gene ID |
M88011  |
| Enzyme 2 GeneCard ID |
GCK  |
| Enzyme 2 GenAtlas ID |
GCK  |
| Enzyme 2 HGNC ID |
HGNC:4195  |
| Enzyme 2 Chromosome Location |
7 |
| Enzyme 2 Locus |
7p15.3-p15.1 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Tanizawa Y, Matsutani A, Chiu KC, Permutt MA: Human glucokinase gene: isolation, structural characterization, and identification of a microsatellite repeat polymorphism. Mol Endocrinol. 1992 Jul;6(7):1070-81. [PubMed
]
- Tanizawa Y, Koranyi LI, Welling CM, Permutt MA: Human liver glucokinase gene: cloning and sequence determination of two alternatively spliced cDNAs. Proc Natl Acad Sci U S A. 1991 Aug 15;88(16):7294-7. [PubMed
]
- Nishi S, Stoffel M, Xiang K, Shows TB, Bell GI, Takeda J: Human pancreatic beta-cell glucokinase: cDNA sequence and localization of the polymorphic gene to chromosome 7, band p 13. Diabetologia. 1992 Aug;35(8):743-7. [PubMed
]
- Koranyi LI, Tanizawa Y, Welling CM, Rabin DU, Permutt MA: Human islet glucokinase gene. Isolation and sequence analysis of full-length cDNA. Diabetes. 1992 Jul;41(7):807-11. [PubMed
]
- Stoffel M, Froguel P, Takeda J, Zouali H, Vionnet N, Nishi S, Weber IT, Harrison RW, Pilkis SJ, Lesage S, et al.: Human glucokinase gene: isolation, characterization, and identification of two missense mutations linked to early-onset non-insulin-dependent (type 2) diabetes mellitus. Proc Natl Acad Sci U S A. 1992 Aug 15;89(16):7698-702. [PubMed
]
- Sakura H, Eto K, Kadowaki H, Simokawa K, Ueno H, Koda N, Fukushima Y, Akanuma Y, Yazaki Y, Kadowaki T: Structure of the human glucokinase gene and identification of a missense mutation in a Japanese patient with early-onset non-insulin-dependent diabetes mellitus. J Clin Endocrinol Metab. 1992 Dec;75(6):1571-3. [PubMed
]
- St Charles R, Harrison RW, Bell GI, Pilkis SJ, Weber IT: Molecular model of human beta-cell glucokinase built by analogy to the crystal structure of yeast hexokinase B. Diabetes. 1994 Jun;43(6):784-91. [PubMed
]
- Stoffel M, Patel P, Lo YM, Hattersley AT, Lucassen AM, Page R, Bell JI, Bell GI, Turner RC, Wainscoat JS: Missense glucokinase mutation in maturity-onset diabetes of the young and mutation screening in late-onset diabetes. Nat Genet. 1992 Oct;2(2):153-6. [PubMed
]
- Chiu KC, Tanizawa Y, Permutt MA: Glucokinase gene variants in the common form of NIDDM. Diabetes. 1993 Apr;42(4):579-82. [PubMed
]
- Stoffel M, Bell KL, Blackburn CL, Powell KL, Seo TS, Takeda J, Vionnet N, Xiang KS, Gidh-Jain M, Pilkis SJ, et al.: Identification of glucokinase mutations in subjects with gestational diabetes mellitus. Diabetes. 1993 Jun;42(6):937-40. [PubMed
]
- Takeda J, Gidh-Jain M, Xu LZ, Froguel P, Velho G, Vaxillaire M, Cohen D, Shimada F, Makino H, Nishi S, et al.: Structure/function studies of human beta-cell glucokinase. Enzymatic properties of a sequence polymorphism, mutations associated with diabetes, and other site-directed mutants. J Biol Chem. 1993 Jul 15;268(20):15200-4. [PubMed
]
- Gidh-Jain M, Takeda J, Xu LZ, Lange AJ, Vionnet N, Stoffel M, Froguel P, Velho G, Sun F, Cohen D, et al.: Glucokinase mutations associated with non-insulin-dependent (type 2) diabetes mellitus have decreased enzymatic activity: implications for structure/function relationships. Proc Natl Acad Sci U S A. 1993 Mar 1;90(5):1932-6. [PubMed
]
- Hager J, Blanche H, Sun F, Vaxillaire NV, Poller W, Cohen D, Czernichow P, Velho G, Robert JJ, Cohen N, et al.: Six mutations in the glucokinase gene identified in MODY by using a nonradioactive sensitive screening technique. Diabetes. 1994 May;43(5):730-3. [PubMed
]
- Velho G, Blanche H, Vaxillaire M, Bellanne-Chantelot C, Pardini VC, Timsit J, Passa P, Deschamps I, Robert JJ, Weber IT, Marotta D, Pilkis SJ, Lipkind GM, Bell GI, Froguel P: Identification of 14 new glucokinase mutations and description of the clinical profile of 42 MODY-2 families. Diabetologia. 1997 Feb;40(2):217-24. [PubMed
]
- Hattersley AT, Beards F, Ballantyne E, Appleton M, Harvey R, Ellard S: Mutations in the glucokinase gene of the fetus result in reduced birth weight. Nat Genet. 1998 Jul;19(3):268-70. [PubMed
]
- Glaser B, Kesavan P, Heyman M, Davis E, Cuesta A, Buchs A, Stanley CA, Thornton PS, Permutt MA, Matschinsky FM, Herold KC: Familial hyperinsulinism caused by an activating glucokinase mutation. N Engl J Med. 1998 Jan 22;338(4):226-30. [PubMed
]
- Ng MC, Cockburn BN, Lindner TH, Yeung VT, Chow CC, So WY, Li JK, Lo YM, Lee ZS, Cockram CS, Critchley JA, Bell GI, Chan JC: Molecular genetics of diabetes mellitus in Chinese subjects: identification of mutations in glucokinase and hepatocyte nuclear factor-1alpha genes in patients with early-onset type 2 diabetes mellitus/MODY. Diabet Med. 1999 Nov;16(11):956-63. [PubMed
]
- Nam JH, Lee HC, Kim YH, Cha BS, Song YD, Lim SK, Kim KR, Huh KB: Identification of glucokinase mutation in subjects with post-renal transplantation diabetes mellitus. Diabetes Res Clin Pract. 2000 Dec;50(3):169-76. [PubMed
]
- Njolstad PR, Sovik O, Cuesta-Munoz A, Bjorkhaug L, Massa O, Barbetti F, Undlien DE, Shiota C, Magnuson MA, Molven A, Matschinsky FM, Bell GI: Neonatal diabetes mellitus due to complete glucokinase deficiency. N Engl J Med. 2001 May 24;344(21):1588-92. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5444 |
| Enzyme 3 Name |
Hexokinase-3 |
| Enzyme 3 Synonyms |
- Hexokinase type III
- HK III
|
| Enzyme 3 Gene Name |
HK3 |
| Enzyme 3 Protein Sequence |
>Hexokinase-3
MDSIGSSGLRQGEETLSCSEEGLPGPSDSSELVQECLQQFKVTRAQLQQIQASLLGSMEQ
ALRGQASPAPAVRMLPTYVGSTPHGTEQGDFVVLELGATGASLRVLWVTLTGIEGHRVEP
RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVNKQGLQLGFSFSFPCHQTGLDRST
LISWTKGFRCSGVEGQDVVQLLRDAIRRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVG
LVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSLSDDGALGPVLTTFDHTLDHESLN
PGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLEHVAEMEDPST
GAARVHAILQDLGLSPGASDVELVQHVCAAVCTRAAQLCAAALAAVLSCLQHSREQQTLQ
VAVATGGRVCERHPRFCSVLQGTVMLLAPECDVSLIPSVDGGGRGVAMVTAVAARLAAHR
RLLEETLAPFRLNHDQLAAVQAQMRKAMAKGLRGEASSLRMLPTFVRATPDGSERGDFLA
LDLGGTNFRVLLVRVTTGVQITSEIYSIPETVAQGSGQQLFDHIVDCIVDFQQKQGLSGQ
SLPLGFTFSFPCRQLGLDQGILLNWTKGFKASDCEGQDVVSLLREAITRRQAVELNVVAI
VNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGD
DGSLAMLSTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGQQIQ
RLQTRDIFKTKFLSEIESDSLALRQVRAILEDLGLPLTSDDALMVLEVCQAVSQRAAQLC
GAGVAAVVEKIRGNRGLEELAVSVGVDGTLYKLHPRFSSLVAATVRELAPRCVVTFLQSE
DGSGKGAALVTAVACRLAQLTRV
|
| Enzyme 3 Number of Residues |
923 |
| Enzyme 3 Molecular Weight |
98921 |
| Enzyme 3 Theoretical pI |
5.11 |
| Enzyme 3 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- hexokinase activity
- nucleotide binding
- phosphotransferase activity, alcohol group as acceptor
- purine nucleotide binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- alcohol metabolism
- cellular metabolism
- glucose catabolism
- glucose metabolism
- glycolysis
- hexose metabolism
- metabolism
- monosaccharide metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 3 General Function |
Not Available |
| Enzyme 3 Specific Function |
ATP + D-hexose = ADP + D-hexose 6-phosphate |
| Enzyme 3 Pathways |
|
| Enzyme 3 Reactions |
- ATP + D-hexose = ADP + D-hexose 6-phosphate
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
1255788  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
P52790  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
HXK3_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>2772 bp
ATGGACTCCATTGGGTCTTCAGGGTTGCGGCAGGGGGAAGAAACCCTGAGTTGCTCTGAG
GAGGGCTTGCCCGGGCCCTCAGACAGCTCAGAGCTGGTGCAGGAGTGCCTGCAGCAGTTC
AAGGTGACAAGGGCACAGCTACAGCAGATCCAAGCCAGCCTCTTGGGTTCCATGGAGCAG
GCGCTGAGGGGACAGGCCAGCCCTGCCCCTGCGGTCCGGATGCTGCCTACATACGTGGGG
TCCACCCCACATGGCACTGAGCAAGGAGACTTCGTGGTGCTGGAGCTGGGGGCCACAGGG
GCCTCACTGCGTGTTTTGTGGGTGACTCTAACTGGCATTGAGGGGCATAGGGTGGAGCCC
AGAAGCCAGGAGTTTGTGATCCCCCAAGAGGTGATGCTGGGTGCTGGCCAGCAGCTCTTT
GACTTTGCTGCCCACTGCCTGTCTGAGTTCCTGGATGCGCAGCCTGTGAACAAACAGGGT
CTGCAGCTTGGCTTCAGCTTCTCTTTCCCTTGTCACCAGACGGGCTTGGACAGGAGCACC
CTCATTTCCTGGACCAAAGGTTTTAGGTGCAGTGGTGTGGAAGGCCAGGATGTGGTCCAG
CTGCTGAGAGATGCCATTCGGAGGCAGGGGGCCTACAACATCGACGTGGTTGCTGTGGTG
AACGACACAGTGGGCACCATGATGGGCTGTGAGCCGGGGGTCAGGCCGTGTGAGGTTGGG
CTAGTTGTAGACACGGGCACCAACGCGTGTTACATGGAGGAGGCACGGCATGTGGCAGTG
CTGGACGAAGACCGGGGCCGCGTCTGCGTCAGCGTCGAGTGGGGCTCCTTAAGCGATGAT
GGGGCGCTGGGACCAGTGCTGACCACCTTCGACCATACCCTGGACCATGAGTCCCTGAAT
CCTGGTGCTCAGAGGTTTGAGAAGATGATCGGAGGCCTGTACCTGGGTGAGCTGGTGCGG
CTGGTGCTGGCTCACTTGGCCCGGTGTGGGGTCCTCTTTGGTGGCTGCACCTCCCCTGCC
CTGCTGAGCCAAGGCAGCATCCTCCTGGAACACGTGGCTGAGATGGAGGACCCCTCTACT
GGGGCAGCCCGTGTCCATGCTATCCTGCAGGACTTGGGCCTGAGCCCTGGGGCTTCGGAT
GTTGAGCTTGTGCAGCACGTCTGTGCGGCCGTGTGCACGCGGGCTGCCCAGCTCTGTGCT
GCCGCCCTGGCCGCTGTTCTCTCCTGCCTCCAGCACAGCCGGGAGCAACAAACACTCCAG
GTTGCTGTGGCCACCGGAGGCCGAGTGTGTGAGCGGCACCCCAGGTTCTGCAGCGTCCTG
CAGGGGACAGTGATGCTCCTGGCCCCGGAATGCGATGTCTCCTTAATCCCCTCTGTGGAT
GGTGGTGGCCGGGGAGTGGCGATGGTGACTGCTGTGGCTGCCCGTCTGGCTGCCCACCGG
CGCCTGCTGGAGGAGACCCTGGCCCCATTCCGGTTGAACCATGATCAACTGGCTGCGGTT
CAGGCACAGATGCGGAAGGCCATGGCCAAGGGGCTCCGAGGGGAGGCCTCCTCCCTTCGC
ATGCTGCCCACTTTCGTCCGGGCCACCCCTGACGGCAGCGAGCGAGGGGATTTCCTGGCC
CTGGACCTCGGGGGCACGAACTTCCGTGTCCTCCTGGTACGTGTGACCACAGGCGTGCAG
ATCACCAGCGAGATCTACTCCATTCCCGAGACTGTGGCCCAGGGTTCTGGGCAGCAGCTC
TTTGACCACATCGTGGACTGCATCGTGGACTTCCAGCAGAAGCAGGGCCTGAGCGGGCAG
AGCCTCCCACTGGGTTTTACCTTCTCCTTCCCATGTAGGCAGCTTGGCCTAGACCAGGGC
ATCCTCCTGAACTGGACCAAGGGTTTCAAGGCATCAGACTGCGAGGGCCAAGATGTCGTG
AGTCTGTTGCGGGAAGCCATCACTCGCAGACAGGCAGTGGAGCTGAATGTGGTTGCCATT
GTCAATGACACGGTGGGGACCATGATGTCCTGTGGCTATGAGGACCCCCGTTGCGAGATA
GGCCTCATTGTCGGAACCGGCACCAATGCCTGCTACATGGAGGAGCTCCGGAATGTGGCG
GGCGTGCCTGGGGACTCAGGCCGCATGTGCATCAACATGGAGTGGGGCGCCTTTGGGGAC
GATGGCTCTCTGGCCATGCTCAGCACCCGCTTTGATGCAAGTGTGGACCAGGCGTCCATC
AACCCCGGCAAGCAGAGGTTTGAAAAGATGATCAGCGGCATGTACCTGGGGGAGATCGTC
CGCCACATCCTTTTACATTTAACCAGCCTTGGCGTTCTCTTCCGGGGCCAGCAGATCCAG
CGCCTTCAGACCAGGGACATCTTCAAGACCAAGTTCCTCTCTGAGATCGAAAGTGACAGC
CTGGCCCTGCGGCAGGTCCGAGCCATCCTAGAGGATCTGGGGCTACCCCTGACCTCAGAT
GACGCCCTGATGGTGCTAGAGGTGTGCCAGGCTGTGTCCCAGAGGGCTGCCCAGCTCTGT
GGGGCGGGTGTAGCTGCCGTGGTGGAGAAGATCCGGGGGAACCGGGGCCTGGAAGAGCTG
GCAGTGTCTGTGGGGGTGGATGGAACGCTCTACAAGCTGCACCCGCGCTTCTCCAGCCTG
GTGGCGGCCACAGTGCGGGAGCTGGCCCCTCGCTGTGTGGTCACGTTCCTGCAGTCAGAG
GATGGGTCCGGCAAAGGTGCGGCCCTGGTCACCGCTGTTGCCTGCCGCCTTGCGCAGTTG
ACTCGTGTCTGA
|
| Enzyme 3 GenBank Gene ID |
U51333  |
| Enzyme 3 GeneCard ID |
HK3  |
| Enzyme 3 GenAtlas ID |
HK3  |
| Enzyme 3 HGNC ID |
HGNC:4925  |
| Enzyme 3 Chromosome Location |
5 |
| Enzyme 3 Locus |
5q35.2 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Furuta H, Nishi S, Le Beau MM, Fernald AA, Yano H, Bell GI: Sequence of human hexokinase III cDNA and assignment of the human hexokinase III gene (HK3) to chromosome band 5q35.2 by fluorescence in situ hybridization. Genomics. 1996 Aug 15;36(1):206-9. [PubMed
]
- Palma F, Agostini D, Mason P, Dacha M, Piccoli G, Biagiarelli B, Fiorani M, Stocchi V: Purification and characterization of the carboxyl-domain of human hexokinase type III expressed as fusion protein. Mol Cell Biochem. 1996 Feb 9;155(1):23-9. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
5445 |
| Enzyme 4 Name |
Hexokinase-2 |
| Enzyme 4 Synonyms |
- Hexokinase type II
- HK II
- Muscle form hexokinase
|
| Enzyme 4 Gene Name |
HK2 |
| Enzyme 4 Protein Sequence |
>Hexokinase-2
MIASHLLAYFFTELNHDQVQKVDQYLYHMRLSDETLLEISKRFRKEMEKGLGATTHPTAA
VKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVTDNGLQKVEMENQIYAIPEDIMR
GSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGV
EGRDVVALIRKAIQRRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGSNACYME
EMRHIDMVEGDEGRMCINMEWGAFGDDGSLNDIRTEFDQEIDMGSLNPGKQLFEKMISGM
YMGELVRLILVKMAKEELLFGGKLSPELLNTGRFETKDISDIEGEKDGIRKAREVLMRLG
LDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKH
PHFAKRLHKTVRRLVPGCDVRFLRSEDGSGKGAAMVTAVAYRLADQHRARQKTLEHLQLS
HDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRV
LLVRVRNGKWGGVEMHNKIYAIPQEVMHGTGDELFDHIVQCIADFLEYMGMKGVSLPLGF
TFSFPCQQNSLDESILLKWTKGFKASGCEGEDVVTLLKEAIHRREEFDLDVVAVVNDTVG
TMMTCGFEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGCLDD
FRTEFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRG
IFETKFLSQIESDCLALLQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAA
VVDRIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHETVKDLAPKCDVSFLQSEDGSGKG
AALITAVACRIREAGQR
|
| Enzyme 4 Number of Residues |
917 |
| Enzyme 4 Molecular Weight |
102381 |
| Enzyme 4 Theoretical pI |
5.93 |
| Enzyme 4 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- hexokinase activity
- nucleotide binding
- phosphotransferase activity, alcohol group as acceptor
- purine nucleotide binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- alcohol metabolism
- cellular metabolism
- glucose catabolism
- glucose metabolism
- glycolysis
- hexose metabolism
- metabolism
- monosaccharide metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 4 General Function |
Not Available |
| Enzyme 4 Specific Function |
ATP + D-hexose = ADP + D-hexose 6-phosphate |
| Enzyme 4 Pathways |
|
| Enzyme 4 Reactions |
- ATP + D-hexose = ADP + D-hexose 6-phosphate
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
587202  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
P52789  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
HXK2_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>2754 bp
ATGATTGCCTCGCATCTGCTTGCCTACTTCTTCACGGAGCTCAACCATGACCAAGTGCAG
AAGGTTGACCAGTATCTCTACCACATGCGCCTCTCTGATGAGACCCTCTTGGAGATCTCT
AAGCGGTTCCGCAAGGAGATGGAGAAAGGGCTTGGAGCCACCACTCACCCTACTGCAGCA
GTGAAGATGCTGCCCACCTTTGTGAGGTCCACTCCAGATGGGACAGAACACGGAGAGTTC
CTGGCTCTGGATCTTGGAGGGACCAACTTCCGTGTGCTTTGGGTGAAAGTAACGGACAAT
GGGCTCCAGAAGGTGGAGATGGAGAATCAGATCTATGCCATCCCTGAGGACATCATGCGA
GGCAGTGGCACCCAGCTGTTTGACCACATTGCCGAATGCCTGGCTAACTTCATGGATAAG
CTACAAATCAAAGACAAGAAGCTCCCACTGGGTTTTACCTTCTCGTTCCCCTGCCACCAG
ACTAAACTAGACGAGAGTTTCCTGGTCTCATGGACCAAGGGATTCAAGTCCAGTGGAGTG
GAAGGCAGAGACGTTGTGGCTCTGATCCGGAAGGCCATCCAGAGGAGAGGGGACTTTGAT
ATCGACATTGTGGCTGTGGTGAATGACACAGTTGGGACCATGATGACCTGTGGTTATGAT
GACCACAACTGTGAGATTGGTCTCATTGTGGGCACGGGCAGCAACGCCTGCTACATGGAA
GAGATGCGCCACATCGACATGGTGGAAGGCGATGAGGGGCGGATGTGTATCAATATGGAG
TGGGGGGCCTTCGGGGACGATGGCTCGCTCAACGACATTCGCACTGAGTTTGACCAGGAG
ATTGACATGGGCTCACTGAACCCGGGAAAGCAACTGTTTGAGAAGATGATCAGTGGGATG
TACATGGGGGAGCTGGTGAGGCTTATCCTGGTGAAGATGGCCAAGGAGGAGCTGCTCTTT
GGGGGGAAGCTCAGCCCAGAGCTTCTCAACACCGGTCGCTTTGAGACCAAAGACATCTCA
GACATTGAAGGGGAGAAGGATGGCATCCGGAAGGCCCGTGAGGTCCTGATGCGGTTGGGC
CTGGACCCGACTCAGGAGGACTGCGTGGCCACTCACCGGATCTGCCAGATCGTGTCCACA
CGCTCCGCCAGCCTGTGCGCAGCCACCCTGGCCGCCGTGCTGCAGCGCATCAAGGAGAAC
AAAGGCGAGGAGCGGCTGCGCTCTACTATTGGGGTCGACGGTTCCGTCTACAAGAAACAC
CCCCATTTTGCCAAGCGTCTACATAAGACCGTGCGGCGGCTGGTGCCCGGCTGCGATGTC
CGCTTCCTCCGCTCCGAGGATGGCAGTGGCAAAGGTGCAGCCATGGTGACAGCAGTGGCT
TACCGGCTGGCCGATCAACACCGTGCCCGCCAGAAGACATTAGAGCATCTGCAGCTGAGC
CATGACCAGCTGCTGGAGGTCAAGAGGAGGATGAAGGTAGAAATGGAGCGAGGTCTGAGC
AAGGAGACTCATGCCAGTGCCCCCGTCAAGATGCTGCCCACCTACGTGTGTGCTACCCCG
GACGGCACAGAGAAAGGGGACTTCTTGGCCTTGGACCTTGGAGGAACAAATTTCCGGGTC
CTGCTGGTCCGTGTTCGGAATGGGAAGTGGGGTGGAGTGGAGATGCACAACAAGATCTAC
GCCATCCCGCAGGAGGTCATGCACGGCACCGGGGACGAGCTCTTTGACCACATTGTCCAG
TGCATCGCGGACTTCCTCGAGTACATGGGCATGAAGGGCGTGTCCCTGCCTCTGGGTTTT
ACCTTCTCCTTCCCCTGCCAGCAGAACAGCCTGGACGAGAGCATCCTCCTCAAGTGGACA
AAAGGCTTCAAGGCATCTGGCTGCGAGGGCGAGGACGTGGTGACCCTGCTGAAGGAAGCG
ATCCACCGGCGAGAGGAGTTTGACCTGGATGTGGTTGCTGTGGTGAACGACACAGTCGGA
ACTATGATGACCTGTGGCTTTGAAGACCCTCACTGTGAAGTTGGCCTCATTGTTGGCACG
GGCAGCAATGCCTGCTACATGGAGGAGATGCGCAACGTGGAACTGGTGGAAGGAGAAGAG
GGGCGGATGTGTGTGAACATGGAATGGGGGGCCTTCGGGGACAATGGATGCCTAGATGAC
TTCCGCACAGAATTTGATGTGGCTGTGGATGAGCTTTCACTCAACCCCGGCAAGCAGAGG
TTCGAGAAAATGATCAGTGGAATGTACCTGGGTGAGATTGTCCGTAACATTCTCATCGAT
TTCACCAAGCGTGGACTACTCTTCCGAGGCCGCATCTCAGAGCGGCTCAAGACAAGGGGC
ATCTTTGAAACCAAGTTCTTGTCTCAGATTGAGAGTGACTGCCTGGCCCTGCTGCAAGTC
CGAGCCACCCTGCAACACTTAGGGCTTGAGAGCACCTGTGACGACAGCATCATTGTTAAG
GAGGTGTGCACTGTGGTGGCCCGGCGGGCAGCCCAGCTCTGTGGCGCAGGCATGGCCGCT
GTGGTGGACAGGATACGAGAAAACCGTGGGCTGGACGCTCTCAAAGTGACAGTGGGTGTG
GATGGGACCCTCTACAAGCTACATCCTCACTTTGCCAAAGTCATGCATGAGACAGTGAAG
GACCTGGCTCCGAAATGTGATGTGTCTTTCCTGCAGTCAGAGGATGGCAGCGGGAAGGGG
GCGGCGCTCATCACTGCTGTGGCCTGCCGCATCCGTGAGGCTGGACAGCGATAG
|
| Enzyme 4 GenBank Gene ID |
Z46376  |
| Enzyme 4 GeneCard ID |
HK2  |
| Enzyme 4 GenAtlas ID |
HK2  |
| Enzyme 4 HGNC ID |
HGNC:4923  |
| Enzyme 4 Chromosome Location |
2 |
| Enzyme 4 Locus |
2p13 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Lehto M, Huang X, Davis EM, Le Beau MM, Laurila E, Eriksson KF, Bell GI, Groop L: Human hexokinase II gene: exon-intron organization, mutation screening in NIDDM, and its relationship to muscle hexokinase activity. Diabetologia. 1995 Dec;38(12):1466-74. [PubMed
]
- Deeb SS, Malkki M, Laakso M: Human hexokinase II: sequence and homology to other hexokinases. Biochem Biophys Res Commun. 1993 Nov 30;197(1):68-74. [PubMed
]
- Shinohara Y, Yamamoto K, Kogure K, Ichihara J, Terada H: Steady state transcript levels of the type II hexokinase and type 1 glucose transporter in human tumor cell lines. Cancer Lett. 1994 Jul 15;82(1):27-32. [PubMed
]
- Laakso M, Malkki M, Deeb SS: Amino acid substitutions in hexokinase II among patients with NIDDM. Diabetes. 1995 Mar;44(3):330-4. [PubMed
]
- Vidal-Puig A, Printz RL, Stratton IM, Granner DK, Moller DE: Analysis of the hexokinase II gene in subjects with insulin resistance and NIDDM and detection of a Gln142-->His substitution. Diabetes. 1995 Mar;44(3):340-6. [PubMed
]
- Echwald SM, Bjorbaek C, Hansen T, Clausen JO, Vestergaard H, Zierath JR, Printz RL, Granner DK, Pedersen O: Identification of four amino acid substitutions in hexokinase II and studies of relationships to NIDDM, glucose effectiveness, and insulin sensitivity. Diabetes. 1995 Mar;44(3):347-53. [PubMed
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
5753 |
| Enzyme 5 Name |
Sorbitol dehydrogenase |
| Enzyme 5 Synonyms |
- L-iditol 2-dehydrogenase
|
| Enzyme 5 Gene Name |
SORD |
| Enzyme 5 Protein Sequence |
>Sorbitol dehydrogenase
MAAAAKPNNLSLVVHGPGDLRLENYPIPEPGPNEVLLRMHSVGICGSDVHYWEYGRIGNF
IVKKPMVLGHEASGTVEKVGSSVKHLKPGDRVAIEPGAPRENDEFCKMGRYNLSPSIFFC
ATPPDDGNLCRFYKHNAAFCYKLPDNVTFEEGALIEPLSVGIHACRRGGVTLGHKVLVCG
AGPIGMVTLLVAKAMGAAQVVVTDLSATRLSKAKEIGADLVLQISKESPQEIARKVEGLL
GCKPEVTIECTGAEASIQAGIYATRSGGTLVLVGLGSEMTTVPLLHAAIREVDIKGVFRY
CNTWPVAISMLASKSVNVKPLVTHRFPLEKALEAFETFKKGLGLKIMLKCDPSDQNP
|
| Enzyme 5 Number of Residues |
357 |
| Enzyme 5 Molecular Weight |
38297 |
| Enzyme 5 Theoretical pI |
8.06 |
| Enzyme 5 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- ion binding
- oxidoreductase activity
- transition metal ion binding
- zinc ion binding
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 5 General Function |
Amino acid transport and metabolism |
| Enzyme 5 Specific Function |
L-iditol + NAD(+) = L-sorbose + NADH |
| Enzyme 5 Pathways |
- Fructose and Mannose Metabolism (map00051
)
|
| Enzyme 5 Reactions |
- L-iditol + NAD+ = L-sorbose + NADH + H+
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
520450  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
Q00796  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
DHSO_HUMAN  |
| Enzyme 5 PDB ID |
1PL8  |
| Enzyme 5 PDB File |
Show |
| Enzyme 5 3D Structure |
|
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>1074 bp
ATGGCGGCGGCGGCCAAGCCCAACAACCTTTCCCTGGTGGTGCACGGACCGGGGGACTTG
CGCCTGGAGAACTATCCTATCCCTGAACCAGGCCCAAATGAGGTCTTGCTGAGGATGCAT
TCTGTTGGAATCTGTGGCTCAGATGTCCACTACTGGGAGTATGGTCGAATTGGGAATTTT
ATTGTGAAAAAGCCCATGGTGCTGGGACATGAAGCTTCGGGAACAGTCGAAAAAGTGGGA
TCATCGGTAAAGCACCTAAAACCAGGTGATCGTGTTGCCATCGAGCCTGGTGCTCCCCGA
GAAAATGATGAATTCTGCAAGATGGGCCGATACAATCTGTCACCTTCCATCTTCTTCTGT
GCCACGCCCCCCGATGACGGGAACCTCTGCCGGTTCTATAAGCACAATGCAGCCTTTTGT
TACAAGCTTCCTGACAATGTCACCTTTGAGGAAGGCGCCCTGATCGAGCCACTTTCTGTG
GGGATCCATGCCTGCAGGAGAGGCGGAGTTACCCTGGGACACAAGGTCCTTGTGTGTGGA
GCTGGGCCAATCGGGATGGTCACTTTGCTCGTGGCCAAAGCAATGGGAGCAGCTCAAGTA
GTGGTGACTGATCTGTCTGCTACCCGATTGTCCAAAGCCAAGGAGATTGGGGCTGATTTA
GTCCTCCAGATCTCCAAGGAGAGCCCTCAGGAAATCGCCAGGAAAGTAGAAGGTCAGCTG
GGGTGCAAGCCGGAAGTCACCATCGAGTGCACGGGGGCAGAGGCCTCCATCCAGGCGGGC
ATCTACGCCACTCGCTCTGGTGGGACCCTCGTGCTTGTGGGGCTGGGCTCTGAGATGACC
ACCGTACCCCTACTGCATGCAGCCATCCGGGAGGTGGATATCAAGGGCGTGTTTCGATAC
TGCAACACGTGGCCAGTGGCGATTTCGATGCTTGCGTCCAAGTCTGTGAATGTAAAACCC
CTCGTCACCCATAGGTTTCCTCTGGAGAAAGCTCTGGAGGCCTTTGAAACATTTAAAAAG
GGATTGGGGTTGAAAATCATGCTCAAGTGTGACCCCAGTGACCAGAATCCCTGA
|
| Enzyme 5 GenBank Gene ID |
U07361  |
| Enzyme 5 GeneCard ID |
SORD  |
| Enzyme 5 GenAtlas ID |
SORD  |
| Enzyme 5 HGNC ID |
HGNC:11184  |
| Enzyme 5 Chromosome Location |
Not Available |
| Enzyme 5 Locus |
Not Available |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Lee FK, Cheung MC, Chung S: The human sorbitol dehydrogenase gene: cDNA cloning, sequence determination, and mapping by fluorescence in situ hybridization. Genomics. 1994 May 15;21(2):354-8. [PubMed
]
- Iwata T, Popescu NC, Zimonjic DB, Karlsson C, Hoog JO, Vaca G, Rodriguez IR, Carper D: Structural organization of the human sorbitol dehydrogenase gene (SORD). Genomics. 1995 Mar 1;26(1):55-62. [PubMed
]
- Carr IM, Markham AF, Coletta PL: Identification and characterisation of a sequence related to human sorbitol dehydrogenase. Eur J Biochem. 1997 May 1;245(3):760-7. [PubMed
]
- Karlsson C, Maret W, Auld DS, Hoog JO, Jornvall H: Variability within mammalian sorbitol dehydrogenases. The primary structure of the human liver enzyme. Eur J Biochem. 1989 Dec 22;186(3):543-50. [PubMed
]
- Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
5997 |
| Enzyme 6 Name |
Alpha-galactosidase A precursor |
| Enzyme 6 Synonyms |
- Melibiase
- Alpha-D- galactoside galactohydrolase
- Alpha-D-galactosidase A
- Agalsidase alfa
|
| Enzyme 6 Gene Name |
GLA |
| Enzyme 6 Protein Sequence |
>Alpha-galactosidase A precursor
MQLRNPELHLGCALALRFLALVSWDIPGARALDNGLARTPTMGWLHWERFMCNLDCQEEP
DSCISEKLFMEMAELMVSEGWKDAGYEYLCIDDCWMAPQRDSEGRLQADPQRFPHGIRQL
ANYVHSKGLKLGIYADVGNKTCAGFPGSFGYYDIDAQTFADWGVDLLKFDGCYCDSLENL
ADGYKHMSLALNRTGRSIVYSCEWPLYMWPFQKPNYTEIRQYCNHWRNFADIDDSWKSIK
SILDWTSFNQERIVDVAGPGGWNDPDMLVIGNFGLSWNQQVTQMALWAIMAAPLFMSNDL
RHISPQAKALLQDKDVIAINQDPLGKQGYQLRQGDNFEVWERPLSGLAWAVAMINRQEIG
GPRSYTIAVASLGKGVACNPACFITQLLPVKRKLGFYEWTSRLRSHINPTGTVLLQLENT
MQMSLKDLL
|
| Enzyme 6 Number of Residues |
429 |
| Enzyme 6 Molecular Weight |
48767 |
| Enzyme 6 Theoretical pI |
5.27 |
| Enzyme 6 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on glycosyl bonds
- hydrolase activity, hydrolyzing O-glycosyl compounds
|
| Process |
- carbohydrate metabolism
- macromolecule metabolism
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 6 General Function |
Not Available |
| Enzyme 6 Specific Function |
Hydrolysis of terminal, non-reducing alpha-D- galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactohydrolase |
| Enzyme 6 Pathways |
|
| Enzyme 6 Reactions |
- Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactohydrolase
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
Not Available |
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
757912  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
P06280  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
AGAL_HUMAN  |
| Enzyme 6 PDB ID |
1R47  |
| Enzyme 6 PDB File |
Show |
| Enzyme 6 3D Structure |
|
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>1290 bp
ATGCAGCTGAGGAACCCAGAACTACATCTGGGCTGCGCGCTTGCGCTTCGCTTCCTGGCC
CTCGTTTCCTGGGACATCCCTGGGGCTAGAGCACTGGACAATGGATTGGCAAGGACGCCT
ACCATGGGCTGGCTGCACTGGGAGCGCTTCATGTGCAACCTTGACTGCCAGGAAGAGCCA
GATTCCTGCATCAGTGAGAAGCTCTTCATGGAGATGGCAGAGCTCATGGTCTCAGAAGGC
TGGAAGGATGCAGGTTATGAGTACCTCTGCATTGATGACTGTTGGATGGCTCCCCAAAGA
GATTCAGAAGGCAGACTTCAGGCAGACCCTCAGCGCTTTCCTCATGGGATTCGCCAGCTA
GCTAATTATGTTCACAGCAAAGGACTGAAGCTAGGGATTTATGCAGATGTTGGAAATAAA
ACCTGCGCAGGCTTCCCTGGGAGTTTTGGATACTACGACATTGATGCCCAGACCTTTGCT
GACTGGGGAGTAGATCTGCTAAAATTTGATGGTTGTTACTGTGACAGTTTGGAAAATTTG
GCAGATGGTTATAAGCACATGTCCTTGGCCCTGAATAGGACTGGCAGAAGCATTGTGTAC
TCCTGTGAGTGGCCTCTTTATATGTGGCCCTTTCAAAAGCCCAATTATACAGAAATCCGA
CAGTACTGCAATCACTGGCGAAATTTTGCTGACATTGATGATTCCTGGAAAAGTATAAAG
AGTATCTTGGACTGGACATCTTTTAACCAGGAGAGAATTGTTGATGTTGCTGGACCAGGG
GGTTGGAATGACCCAGATATGTTAGTGATTGGCAACTTTGGCCTCAGCTGGAATCAGCAA
GTAACTCAGATGGCCCTCTGGGCTATCATGGCTGCTCCTTTATTCATGTCTAATGACCTC
CGACACATCAGCCCTCAAGCCAAAGCTCTCCTTCAGGATAAGGACGTAATTGCCATCAAT
CAGGACCCCTTGGGCAAGCAAGGGTACCAGCTTAGACAGGGAGACAACTTTGAAGTGTGG
GAACGACCTCTCTCAGGCTTAGCCTGGGCTGTAGCTATGATAAACCGGCAGGAGATTGGT
GGACCTCGCTCTTATACCATCGCAGTTGCTTCCCTGGGTAAAGGAGTGGCCTGTAATCCT
GCCTGCTTCATCACACAGCTCCTCCCTGTGAAAAGGAAGCTAGGGTTCTATGAATGGACT
TCAAGGTTAAGAAGTCACATAAATCCCACAGGCACTGTTTTGCTTCAGCTAGAAAATACA
ATGCAGATGTCATTAAAAGACTTACTTTAA
|
| Enzyme 6 GenBank Gene ID |
X05790  |
| Enzyme 6 GeneCard ID |
GLA  |
| Enzyme 6 GenAtlas ID |
GLA  |
| Enzyme 6 HGNC ID |
HGNC:4296  |
| Enzyme 6 Chromosome Location |
X |
| Enzyme 6 Locus |
Xq22 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- Tsuji S, Martin BM, Kaslow DC, Migeon BR, Choudary PV, Stubbleflied BK, Mayor JA, Murray GJ, Barranger JA, Ginns EI: Signal sequence and DNA-mediated expression of human lysosomal alpha-galactosidase A. Eur J Biochem. 1987 Jun 1;165(2):275-80. [PubMed
]
- Kornreich R, Desnick RJ, Bishop DF: Nucleotide sequence of the human alpha-galactosidase A gene. Nucleic Acids Res. 1989 Apr 25;17(8):3301-2. [PubMed
]
- Oeltjen JC, Liu X, Lu J, Allen RC, Muzny D, Belmont JW, Gibbs RA: Sixty-nine kilobases of contiguous human genomic sequence containing the alpha-galactosidase A and Bruton's tyrosine kinase loci. Mamm Genome. 1995 May;6(5):334-8. [PubMed
]
- Bishop DF, Calhoun DH, Bernstein HS, Hantzopoulos P, Quinn M, Desnick RJ: Human alpha-galactosidase A: nucleotide sequence of a cDNA clone encoding the mature enzyme. Proc Natl Acad Sci U S A. 1986 Jul;83(13):4859-63. [PubMed
]
- Quinn M, Hantzopoulos P, Fidanza V, Calhoun DH: A genomic clone containing the promoter for the gene encoding the human lysosomal enzyme, alpha-galactosidase A. Gene. 1987;58(2-3):177-88. [PubMed
]
- Bishop DF, Kornreich R, Desnick RJ: Structural organization of the human alpha-galactosidase A gene: further evidence for the absence of a 3' untranslated region. Proc Natl Acad Sci U S A. 1988 Jun;85(11):3903-7. [PubMed
]
- Novo FJ, Kruszewski A, MacDermot KD, Goldspink G, Gorecki DC: Editing of human alpha-galactosidase RNA resulting in a pyrimidine to purine conversion. Nucleic Acids Res. 1995 Jul 25;23(14):2636-40. [PubMed
]
- Eng CM, Desnick RJ: Molecular basis of Fabry disease: mutations and polymorphisms in the human alpha-galactosidase A gene. Hum Mutat. 1994;3(2):103-11. [PubMed
]
- Koide T, Ishiura M, Iwai K, Inoue M, Kaneda Y, Okada Y, Uchida T: A case of Fabry's disease in a patient with no alpha-galactosidase A activity caused by a single amino acid substitution of Pro-40 by Ser. FEBS Lett. 1990 Jan 1;259(2):353-6. [PubMed
]
- von Scheidt W, Eng CM, Fitzmaurice TF, Erdmann E, Hubner G, Olsen EG, Christomanou H, Kandolf R, Bishop DF, Desnick RJ: An atypical variant of Fabry's disease with manifestations confined to the myocardium. N Engl J Med. 1991 Feb 7;324(6):395-9. [PubMed
]
- Sakuraba H, Oshima A, Fukuhara Y, Shimmoto M, Nagao Y, Bishop DF, Desnick RJ, Suzuki Y: Identification of point mutations in the alpha-galactosidase A gene in classical and atypical hemizygotes with Fabry disease. Am J Hum Genet. 1990 Nov;47(5):784-9. [PubMed
]
- Bernstein HS, Bishop DF, Astrin KH, Kornreich R, Eng CM, Sakuraba H, Desnick RJ: Fabry disease: six gene rearrangements and an exonic point mutation in the alpha-galactosidase gene. J Clin Invest. 1989 Apr;83(4):1390-9. [PubMed
]
- Ishii S, Sakuraba H, Suzuki Y: Point mutations in the upstream region of the alpha-galactosidase A gene exon 6 in an atypical variant of Fabry disease. Hum Genet. 1992 Apr;89(1):29-32. [PubMed
]
- Eng CM, Resnick-Silverman LA, Niehaus DJ, Astrin KH, Desnick RJ: Nature and frequency of mutations in the alpha-galactosidase A gene that cause Fabry disease. Am J Hum Genet. 1993 Dec;53(6):1186-97. [PubMed
]
- Davies JP, Winchester BG, Malcolm S: Mutation analysis in patients with the typical form of Anderson-Fabry disease. Hum Mol Genet. 1993 Jul;2(7):1051-3. [PubMed
]
- Davies J, Christomanou H, Winchester B, Malcolm S: Detection of 8 new mutations in the alpha-galactosidase A gene in Fabry disease. Hum Mol Genet. 1994 Apr;3(4):667-9. [PubMed
]
- Eng CM, Niehaus DJ, Enriquez AL, Burgert TS, Ludman MD, Desnick RJ: Fabry disease: twenty-three mutations including sense and antisense CpG alterations and identification of a deletional hot-spot in the alpha-galactosidase A gene. Hum Mol Genet. 1994 Oct;3(10):1795-9. [PubMed
]
- Okumiya T, Ishii S, Takenaka T, Kase R, Kamei S, Sakuraba H, Suzuki Y: Galactose stabilizes various missense mutants of alpha-galactosidase in Fabry disease. Biochem Biophys Res Commun. 1995 Sep 25;214(3):1219-24. [PubMed
]
- Okumiya T, Ishii S, Kase R, Kamei S, Sakuraba H, Suzuki Y: Alpha-galactosidase gene mutations in Fabry disease: heterogeneous expressions of mutant enzyme proteins. Hum Genet. 1995 May;95(5):557-61. [PubMed
]
- Madsen KM, Hasholt L, Sorensen SA, Fermer ML, Dahl N: Two novel mutations (L32P) and (G85N) among five different missense mutations in six Danish families with Fabry's disease. Hum Mutat. 1995;5(3):277-8. [PubMed
]
- Nakao S, Takenaka T, Maeda M, Kodama C, Tanaka A, Tahara M, Yoshida A, Kuriyama M, Hayashibe H, Sakuraba H, et al.: An atypical variant of Fabry's disease in men with left ventricular hypertrophy. N Engl J Med. 1995 Aug 3;333(5):288-93. [PubMed
]
- Davies JP, Eng CM, Hill JA, Malcolm S, MacDermot K, Winchester B, Desnick RJ: Fabry disease: fourteen alpha-galactosidase A mutations in unrelated families from the United Kingdom and other European countries. Eur J Hum Genet. 1996;4(4):219-24. [PubMed
]
- Cariolou MA, Christodoulides M, Manoli P, Kokkofitou A, Tsambaos D: Novel trinucleotide deletion in Fabry's disease. Hum Genet. 1996 Apr;97(4):468-70. [PubMed
]
- Germain D, Biasotto M, Tosi M, Meo T, Kahn A, Poenaru L: Fluorescence-assisted mismatch analysis (FAMA) for exhaustive screening of the alpha-galactosidase A gene and detection of carriers in Fabry disease. Hum Genet. 1996 Dec;98(6):719-26. [PubMed
]
- Blanch LC, Meaney C, Morris CP: A sensitive mutation screening strategy for Fabry disease: detection of nine mutations in the alpha-galactosidase A gene. Hum Mutat. 1996;8(1):38-43. [PubMed
]
- Redonnet-Vernhet I, Ploos van Amstel JK, Jansen RP, Wevers RA, Salvayre R, Levade T: Uneven X inactivation in a female monozygotic twin pair with Fabry disease and discordant expression of a novel mutation in the alpha-galactosidase A gene. J Med Genet. 1996 Aug;33(8):682-8. [PubMed
]
- Takata T, Okumiya T, Hayashibe H, Shimmoto M, Kase R, Itoh K, Utsumi K, Kamei S, Sakuraba H: Screening and detection of gene mutations in Japanese patients with Fabry disease by non-radioactive single-stranded conformation polymorphism analysis. Brain Dev. 1997 Mar;19(2):111-6. [PubMed
]
- Eng CM, Ashley GA, Burgert TS, Enriquez AL, D'Souza M, Desnick RJ: Fabry disease: thirty-five mutations in the alpha-galactosidase A gene in patients with classic and variant phenotypes. Mol Med. 1997 Mar;3(3):174-82. [PubMed
]
- Miyazaki T, Kajita M, Ohmori S, Mizutani N, Niwa T, Murata Y, Seo H: A novel mutation (E358K) in the alpha-galactosidase A gene detected in a Japanese family with Fabry disease. Hum Mutat. 1998;Suppl 1:S139-40. [PubMed
]
- Okumiya T, Kawamura O, Itoh K, Kase R, Ishii S, Kamei S, Sakuraba H: Novel missense mutation (M72V) of alpha-galactosidase gene and its expression product in an atypical Fabry hemizygote. Hum Mutat. 1998;Suppl 1:S213-6. [PubMed
]
- Guffon N, Froissart R, Chevalier-Porst F, Maire I: Mutation analysis in 11 French patients with Fabry disease. Hum Mutat. 1998;Suppl 1:S288-90. [PubMed
]
- Germain DP, Poenaru L: Fabry disease: identification of novel alpha-galactosidase A mutations and molecular carrier detection by use of fluorescent chemical cleavage of mismatches. Biochem Biophys Res Commun. 1999 Apr 21;257(3):708-13. [PubMed
]
- Beyer EM, Karpova EA, Udalova OV, Ploos van Amstel JK, van Diggelen OP, Tsvetkova IV: The multiple cases of Fabry disease in a Russian family caused by an E341K amino acid substitution in the alpha-galactosidase A. Clin Chim Acta. 1999 Feb;280(1-2):81-9. [PubMed
]
- Topaloglu AK, Ashley GA, Tong B, Shabbeer J, Astrin KH, Eng CM, Desnick RJ: Twenty novel mutations in the alpha-galactosidase A gene causing Fabry disease. Mol Med. 1999 Dec;5(12):806-11. [PubMed
]
- Lee JK, Kim GH, Kim JS, Kim KK, Lee MC, Yoo HW: Identification of four novel mutations in five unrelated Korean families with Fabry disease. Clin Genet. 2000 Sep;58(3):228-33. [PubMed
]
- Ashton-Prolla P, Tong B, Shabbeer J, Astrin KH, Eng CM, Desnick RJ: Fabry disease: twenty-two novel mutations in the alpha-galactosidase A gene and genotype/phenotype correlations in severely and mildly affected hemizygotes and heterozygotes. J Investig Med. 2000 Jul;48(4):227-35. [PubMed
]
- Germain DP, Salard D, Fellmann F, Azibi K, Caillaud C, Bernard MC, Poenaru L: Identification of a novel de novo mutation (G373D) in the alpha-galactosidase A gene (GLA) in a patient affected with Fabry disease. Hum Mutat. 2001 Apr;17(4):353. [PubMed
]
- Blaydon D, Hill J, Winchester B: Fabry disease: 20 novel GLA mutations in 35 families. Hum Mutat. 2001 Nov;18(5):459. [PubMed
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
7418 |
| Enzyme 7 Name |
Glycophorin B precursor |
| Enzyme 7 Synonyms |
- PAS-3
- Sialoglycoprotein delta
- SS-active sialoglycoprotein
- CD235b antigen
|
| Enzyme 7 Gene Name |
GYPB |
| Enzyme 7 Protein Sequence |
>Glycophorin B precursor
MYGKIIFVLLLSEIVSISALSTTEVAMHTSTSSSVTKSYISSQTNGETGQLVHRFTVPAP
VVIILIILCVMAGIIGTILLISYTIRRLIKA
|
| Enzyme 7 Number of Residues |
91 |
| Enzyme 7 Molecular Weight |
9796 |
| Enzyme 7 Theoretical pI |
9.73 |
| Enzyme 7 GO Classification |
| Function |
| — |
| Process |
| — |
| Component |
|
|
| Enzyme 7 General Function |
Not Available |
| Enzyme 7 Specific Function |
This protein is a minor sialoglycoprotein in erythrocyte membranes |
| Enzyme 7 Pathways |
Not Available |
| Enzyme 7 Reactions |
Not Available |
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
183313  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
P06028  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
GLPB_HUMAN  |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>276 bp
ATGTATGGAAAAATAATCTTTGTATTACTATTGTCAGAAATTGTGAGCATATCAGCATTA
AGTACCACTGAGGTGGCAATGCACACTTCAACCTCTTCTTCAGTCACAAAGAGTTACATC
TCATCACAGACAAATGGAGAAACGGGACAACTTGTCCATCGTTTCACTGTACCAGCTCCT
GTAGTGATAATACTCATTATTTTGTGTGTGATGGCTGGTATTATTGGAACGATCCTCTTA
ATTTCTTACACTATTCGCCGACTGATAAAGGCATGA
|
| Enzyme 7 GenBank Gene ID |
J02982  |
| Enzyme 7 GeneCard ID |
GYPB  |
| Enzyme 7 GenAtlas ID |
GYPB  |
| Enzyme 7 HGNC ID |
HGNC:4703  |
| Enzyme 7 Chromosome Location |
4 |
| Enzyme 7 Locus |
4q28-q31 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- Siebert PD, Fukuda M: Molecular cloning of a human glycophorin B cDNA: nucleotide sequence and genomic relationship to glycophorin A. Proc Natl Acad Sci U S A. 1987 Oct;84(19):6735-9. [PubMed
]
- Tate CG, Tanner MJ: Isolation of cDNA clones for human erythrocyte membrane sialoglycoproteins alpha and delta. Biochem J. 1988 Sep 15;254(3):743-50. [PubMed
]
- Kudo S, Fukuda M: Structural organization of glycophorin A and B genes: glycophorin B gene evolved by homologous recombination at Alu repeat sequences. Proc Natl Acad Sci U S A. 1989 Jun;86(12):4619-23. [PubMed
]
- Huang CH, Blumenfeld OO: Molecular genetics of human erythrocyte MiIII and MiVI glycophorins. Use of a pseudoexon in construction of two delta-alpha-delta hybrid genes resulting in antigenic diversification. J Biol Chem. 1991 Apr 15;266(11):7248-55. [PubMed
]
- Blanchard D, Dahr W, Hummel M, Latron F, Beyreuther K, Cartron JP: Glycophorins B and C from human erythrocyte membranes. Purification and sequence analysis. J Biol Chem. 1987 Apr 25;262(12):5808-11. [PubMed
]
- Dahr W, Beyreuther K, Moulds J, Unger P: Hybrid glycophorins from human erythrocyte membranes. I. Isolation and complete structural analysis of the hybrid sialoglycoprotein from Dantu-positive red cells of the N.E. variety. Eur J Biochem. 1987 Jul 1;166(1):31-6. [PubMed
]
- Huang CH, Spruell P, Moulds JJ, Blumenfeld OO: Molecular basis for the human erythrocyte glycophorin specifying the Miltenberger class I (MiI) phenotype. Blood. 1992 Jul 1;80(1):257-63. [PubMed
]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
15209 |
| Enzyme 8 Name |
cDNA FLJ78173, highly similar to Homo sapiens hexokinase 1 (HK1) mRNA |
| Enzyme 8 Synonyms |
Not Available |
| Enzyme 8 Gene Name |
Not Available |
| Enzyme 8 Protein Sequence |
>cDNA FLJ78173, highly similar to Homo sapiens hexokinase 1 (HK1) mRNA
MIAAQLLAYYFTELKDDQVKKIDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDFNPTAT
VKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVHMESEVYDTPENIVH
GSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGV
EGADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYME
ELRHIDLVEGDEGRMCINTEWGAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGM
YLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKNKEGLHNAKEILTRLG
VEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTH
PQYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRLAEQHRQIEETLAHFHLT
KDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRRTPDGTENGDFLALDLGGTNFRV
LLVKIRSGKKRTVEMHNKIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGF
TFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVTLLRDAIKRREEFDLDVVAVVNDTVG
TMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGCLDD
IRTHYDRLVDEYSLNAGKQGYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRG
IFETKFLSQIESDRLALLQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAA
VVDKIRENRGLDRLNVTVGVDGTLYKLHPHFSRIMHQTVKELSPKCNVSFLLSEDGSGKG
AALITAVGVRLRTEASS
|
| Enzyme 8 Number of Residues |
917 |
| Enzyme 8 Molecular Weight |
102388 |
| Enzyme 8 Theoretical pI |
6.70 |
| Enzyme 8 GO Classification |
Not Available |
| Enzyme 8 General Function |
Not Available |
| Enzyme 8 Specific Function |
Not Available |
| Enzyme 8 Pathways |
Not Available |
| Enzyme 8 Reactions |
Not Available |
| Enzyme 8 Pfam Domain Function |
Not Available |
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
158257456  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
A8K7J7  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
A8K7J7_HUMAN  |
| Enzyme 8 PDB ID |
1HKB  |
| Enzyme 8 PDB File |
Show |
| Enzyme 8 3D Structure |
|
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>2754 bp
ATGATCGCCGCGCAGCTCCTGGCCTATTACTTCACGGAGCTGAAGGATGACCAGGTCAAA
AAGATTGACAAGTATCTGTATGCCATGCGGCTCTCCGATGAAACTCTCATAGATATCATG
ACTCGCTTCAGGAAGGAGATGAAGAATGGCCTCTCCCGGGATTTTAATCCAACAGCCACA
GTCAAGATGTTGCCAACATTCGTAAGGTCCATTCCTGATGGCTCTGAAAAGGGAGATTTC
ATTGCCCTGGATCTTGGTGGGTCTTCCTTTCGAATTCTGCGGGTGCAAGTGAATCATGAG
AAAAACCAGAATGTTCACATGGAGTCCGAGGTTTATGACACCCCAGAGAACATCGTGCAC
GGCAGTGGAAGCCAGCTTTTTGATCATGTTGCTGAGTGCCTGGGAGATTTCATGGAGAAA
AGGAAGATCAAGGACAAGAAGTTACCTGTGGGATTCACGTTTTCTTTTCCTTGCCAACAA
TCCAAAATAGATGAGGCCATCCTGATCACCTGGACAAAGCGATTTAAAGCGAGCGGAGTG
GAAGGAGCAGATGTGGTCAAACTGCTTAACAAAGCCATCAAAAAGCGAGGGGACTATGAT
GCCAACATCGTAGCTGTGGTGAATGACACAGTGGGCACCATGATGACCTGTGGCTATGAC
GACCAGCACTGTGAAGTCGGCCTGATCATCGGCACTGGCACCAATGCTTGCTACATGGAG
GAACTGAGGCACATTGATCTGGTGGAAGGAGACGAGGGGAGGATGTGTATCAATACAGAA
TGGGGAGCCTTTGGAGACGATGGATCATTAGAAGACATCCGGACAGAGTTTGACAGGGAG
ATAGACCGGGGATCCCTCAACCCTGGAAAACAGCTGTTTGAGAAGATGGTCAGTGGCATG
TACTTGGGAGAGCTGGTTCGACTGATCCTAGTCAAGATGGCCAAGGAGGGCCTCTTATTT
GAAGGGCGGATCACCCCGGAGCTGCTCACCCGAGGGAAGTTTAACACCAGTGATGTGTCA
GCCATCGAAAAGAATAAGGAAGGCCTCCACAATGCCAAAGAAATCCTGACCCGCCTGGGA
GTGGAGCCGTCCGATGATGACTGTGTCTCAGTCCAGCACGTTTGCACCATTGTCTCATTT
CGCTCAGCCAACTTGGTGGCTGCCACACTGGGCGCCATCTTGAACCGCCTGCGTGATAAC
AAGGGCACACCCAGGCTGCGGACCACGGTTGGTGTCGACGGATCTCTTTACAAGACGCAC
CCACAGTATTCCCGGCGTTTCCACAAGACTCTAAGGCGCTTGGTGCCAGACTCCGATGTG
CGCTTCCTCCTCTCGGAGAGTGGCAGCGGCAAGGGGGCTGCCATGGTGACGGCGGTGGCC
TACCGCTTGGCCGAGCAGCACCGGCAGATAGAGGAGACCCTGGCTCATTTCCACCTCACC
AAAGACATGCTGCTGGAGGTGAAGAAGAGGATGCGGGCCGAGATGGAGCTGGGGCTGAGG
AAGCAGACGCACAACAATGCCGTGGTTAAGATGCTGCCCTCCTTCGTCCGGAGAACTCCC
GACGGGACCGAGAATGGTGACTTCTTGGCCCTGGATCTTGGAGGAACCAATTTCCGTGTG
CTGCTGGTGAAAATCCGTAGTGGGAAAAAGAGAACGGTGGAAATGCACAACAAGATCTAC
GCCATTCCTATTGAAATCATGCAGGGCACTGGGGAAGAGCTGTTTGATCACATTGTCTCC
TGCATCTCTGACTTCTTGGACTACATGGGGATCAAAGGCCCCAGGATGCCTCTGGGCTTC
ACGTTCTCATTTCCCTGCCAGCAGACGAGTCTGGACGCGGGAATCTTGATCACGTGGACA
AAGGGTTTTAAGGCAACAGACTGCGTGGGCCACGATGTAGTCACCTTACTAAGGGATGCG
ATAAAAAGGAGAGAGGAATTTGACCTGGACGTGGTGGCTGTGGTCAACGACACAGTGGGC
ACCATGATGACCTGTGCTTATGAGGAGCCCACCTGTGAGGTTGGACTCATTGTTGGGACC
GGCAGCAATGCCTGCTACATGGAGGAGATGAAGAACGTGGAGATGGTGGAGGGGGACCAG
GGGCAGATGTGCATCAACATGGAGTGGGGGGCCTTTGGGGACAACGGGTGTCTGGATGAT
ATCAGGACACACTACGACAGACTGGTGGACGAATATTCCCTAAATGCTGGGAAACAAGGG
TATGAGAAGATGATCAGTGGTATGTACCTGGGTGAAATCGTCCGCAACATCTTAATCGAC
TTCACCAAGAAGGGATTCCTCTTCCGAGGGCAGATCTCTGAGACGCTGAAGACCCGGGGC
ATCTTTGAGACCAAGTTTCTCTCTCAGATCGAGAGTGACCGATTAGCACTGCTCCAGGTC
CGGGCTATCCTCCAGCAGCTAGGTCTGAATAGCACCTGCGATGACAGTATCCTCGTCAAG
ACAGTGTGCGGGGTGGTGTCCAGGAGGGCCGCACAGCTGTGTGGCGCAGGCATGGCTGCG
GTTGTGGATAAGATCCGCGAGAACAGAGGACTGGACCGTCTGAATGTGACTGTGGGAGTG
GACGGGACACTCTACAAGCTTCATCCACACTTCTCCAGAATCATGCACCAGACGGTGAAG
GAACTGTCACCAAAATGTAACGTGTCCTTCCTCCTGTCTGAGGATGGCAGCGGCAAGGGG
GCCGCCCTCATCACGGCCGTGGGCGTGCGGTTACGCACAGAGGCAAGCAGCTAA
|
| Enzyme 8 GenBank Gene ID |
AK292012  |
| Enzyme 8 GeneCard ID |
A8K7J7  |
| Enzyme 8 GenAtlas ID |
Not Available |
| Enzyme 8 HGNC ID |
Not Available |
| Enzyme 8 Chromosome Location |
Not Available |
| Enzyme 8 Locus |
Not Available |
| Enzyme 8 SNPs |
Not Available |
| Enzyme 8 General References |
Not Available |
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
16486 |
| Enzyme 9 Name |
cDNA, FLJ93978, Homo sapiens aldo-keto reductase family 1, member B1 (aldosereductase) (AKR1B1), mRNA (Aldo-keto reductase family 1, member B1 (Aldose reductase), isoform CRA_a) |
| Enzyme 9 Synonyms |
Not Available |
| Enzyme 9 Gene Name |
AKR1B1 |
| Enzyme 9 Protein Sequence |
>cDNA, FLJ93978, Homo sapiens aldo-keto reductase family 1, member B1 (aldosereductase) (AKR1B1), mRNA (Aldo-keto reductase family 1, member B1 (Aldose reductase), isoform CRA_a)
MASRLLLNNGAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQ
EKLREQVVKREELFIVSKLWCTYHEKGLVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGK
EFFPLDESGNVVPSDTNILDTWAAMEELVDEGLVKAIGISNFNHLQVEMILNKPGLKYKP
AVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPRIKAIAAK
HNKTTAQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTLLSYNRNWRVCA
LLSCTSHKDYPFHEEF
|
| Enzyme 9 Number of Residues |
316 |
| Enzyme 9 Molecular Weight |
35854 |
| Enzyme 9 Theoretical pI |
6.99 |
| Enzyme 9 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 9 General Function |
Not Available |
| Enzyme 9 Specific Function |
Not Available |
| Enzyme 9 Pathways |
Not Available |
| Enzyme 9 Reactions |
Not Available |
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
Not Available |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
B2R8N3  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
B2R8N3_HUMAN  |
| Enzyme 9 PDB ID |
1T40  |
| Enzyme 9 PDB File |
Show |
| Enzyme 9 3D Structure |
|
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
Not Available |
| Enzyme 9 GenBank Gene ID |
AK313439  |
| Enzyme 9 GeneCard ID |
B2R8N3  |
| Enzyme 9 GenAtlas ID |
Not Available |
| Enzyme 9 HGNC ID |
Not Available |
| Enzyme 9 Chromosome Location |
Not Available |
| Enzyme 9 Locus |
Not Available |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
Not Available |
| Enzyme 9 Metabolite References |
Not Available |