| Version |
2.5 |
| Creation Date |
2005-11-16 15:48:42 |
| Update Date |
2009-06-01 10:58:18 |
| Accession Number |
HMDB00807 |
| Secondary Accession Numbers |
Not Available |
| Common Name |
3-Phosphoglyceric acid |
| Description |
3-phosphoglyceric acid (3PG) is a 3-carbon molecule that is a metabolic intermediate in both glycolysis and the Calvin cycle. This chemical is often termed PGA when referring to the Calvin cycle. In the Calvin cycle, two glycerate 3-phosphate molecules are reduced to form two molecules of glyceraldehyde 3-phosphate (GALP). (wikipedia) |
| Synonyms |
- 3-(dihydrogen phosphate)Glycerate
- 3-(dihydrogen phosphate)Glyceric acid
- 3-Glycerophosphorate
- 3-Glycerophosphoric acid
- 3-P-D-glycerate
- 3-P-glycerate
- 3-PGA
- 3-Phosphoglycerate
- 3-Phosphoglyceric acid
- 3-pg
- 3-phospho-(R)-glycerate
- 3-phospho-D-glycerate
- 3-phospho-glycerate
- 3-phospho-glyceric acid
- D-Glycerate 3-phosphate
- G3P
- Glycerate 3-phosphate
- Glyceric acid 3-phosphate
- Phosphoglycerate
- glycerate-3-P
- D-(-)-3-Phosphoglyceric acid
|
| Chemical IUPAC Name |
2-hydroxy-3-phosphonooxy-propanoic acid |
| Chemical Formula |
C3H7O7P |
| Chemical Structure |
 |
| Chemical Taxonomy |
| Kingdom |
|
| Super Class |
|
| Class |
|
| Sub Class |
|
| Family |
|
| Species |
- secondary alcohol
- carboxylic acid
- phosphoric acid ester
- alpha-hydroxyacid
|
| Biofunction |
- Component of Glycine, serine and threonine metabolism
|
| Application |
| — |
| Source |
|
|
| Average Molecular Weight |
186.057 |
| Monoisotopic Molecular Weight |
185.992935 |
| Isomeric SMILES |
OC(COP(O)(O)=O)C(O)=O |
| Canonical SMILES |
OC(COP(O)(O)=O)C(O)=O |
| KEGG Compound ID |
C00597  |
| BioCyc ID |
G3P  |
| BiGG ID |
34230  |
| Wikipedia Link |
3-Phosphoglycerate  |
| NuGOwiki Link |
HMDB00807  |
| Metagene Link |
HMDB00807  |
| METLIN ID |
150  |
| PubChem Compound |
724  |
| PubChem Substance |
8144701  |
| ChEBI ID |
17050  |
| CAS Registry Number |
820-11-1 |
| InChI Identifier |
InChI=1/C3H7O7P/c4-2(3(5)6)1-10-11(7,8)9/h2,4H,1H2,(H,5,6)(H2,7,8,9) |
| Synthesis Reference |
Jakoby, Wm. B.; Brummond, Dewey O.; Ochoa, Severo. Formation of 3-phosphoglyceric acid by carbon dioxide fixation with spinach-leaf enzymes. Journal of Biological Chemistry (1956), 218 811-22. |
| Melting Point (Experimental) |
Not Available |
| Experimental Water Solubility |
Not Available
Source: PhysProp
|
| Predicted Water Solubility |
21.0 mg/mL [Predicted by ALOGPS]
Calculated using ALOGPS
|
| Physiological Charge |
-3 |
| State |
Solid |
| Experimental LogP/Hydrophobicity |
Not Available
Source: PhysProp
|
| Predicted LogP/Hydrophobicity |
-2.26 [Predicted by ALOGPS]; -3 [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 |
13PK  |
| Experimental PDB File |
Show |
| Experimental PDB Structure |
|
| Experimental 1H NMR Spectrum |
Download Spectrum Download FID (Bruker) Show Experimental Conditions  |
| Experimental 13C NMR Spectrum |
Not Available |
| 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 |
|
| Tissue Location |
Not Available |
| Concentrations (Normal) |
| Biofluid |
Blood |
| Value |
58.2 +/- 14.4 uM |
| Age |
Newborn:0-30 days 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 |
Blood |
| Value |
47.2 +/- 7.4 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 |
Cellular Cytoplasm |
| Value |
45 uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Nakayama Y, Kinoshita A, Tomita M: Dynamic simulation of red blood cell metabolism and its application to the analysis of a pathological condition. Theor Biol Med Model. 2005 May 9;2(1):18. [PubMed
]
|
|
| Concentrations (Abnormal) |
Not Available |
| Associated Disorders |
Not Available |
| OMIM ID |
Not Available |
| Pathways |
|
| General References |
- Yu KT, Pendley C 2nd, Herczeg T, Pendleton RG: 2,3-Diphosphoglycerate phosphatase/synthase: a potential target for elevating the diphosphoglycerate level in human red blood cells. J Pharmacol Exp Ther. 1990 Jan;252(1):192-200. [PubMed
]
- Uchida K, Kondoh K, Matuo Y: Recombinant M-, B- and MB-type isozymes of human phosphoglyceric acid mutase: their large-scale production and preparation of polyclonal antibodies specific to M- and B-type isozymes. Clin Chim Acta. 1995 Jun 15;237(1-2):43-58. [PubMed
]
- Uchida K, Mori K, Matuo Y: [Phosphoglyceric acid mutase] Nippon Rinsho. 1995 May;53(5):1247-52. [PubMed
]
- Nakai A, Shigematsu Y, Liu YY, Kikawa Y, Sudo M: Urinary sugar phosphates and related organic acids in fructose-1,6-diphosphatase deficiency. J Inherit Metab Dis. 1993;16(2):408-14. [PubMed
]
- Sayed A, Matsuyama S, Inoue K, Alsina J, Cai F, Chen J, Inouye M: ATPase and GTPase activities copurifying with GTP-binding proteins in E. coli. J Mol Microbiol Biotechnol. 2000 Jul;2(3):261-3. [PubMed
]
- Grisolia S, Salinas M, Wallace R, Singh GK: Influence of size, protein concentration, protein synthesis inhibitors,and carbon on clearance of enzymes and proteins from blood. Physiol Chem Phys. 1976;8(1):37-52. [PubMed
]
- Mair J: Progress in myocardial damage detection: new biochemical markers for clinicians. Crit Rev Clin Lab Sci. 1997;34(1):1-66. [PubMed
]
- Nakayama Y, Kinoshita A, Tomita M: Dynamic simulation of red blood cell metabolism and its application to the analysis of a pathological condition. Theor Biol Med Model. 2005 May 9;2(1):18. [PubMed
]
- Glaus M, Schneider W: Iron release from transferrin induced by mixed ligand complexes of copper(II). Biol Met. 1989;2(3):185-90. [PubMed
]
- Mayo Medical Laboratories 2005 Test Catalog
- Veech RL, Lawson JW, Cornell NW, Krebs HA: Cytosolic phosphorylation potential. J Biol Chem. 1979 Jul 25;254(14):6538-47. [PubMed
]
- Wikipedia

|
| Metabolic Enzymes |
- Bisphosphoglycerate mutase
- Phosphoglycerate mutase 1
- Acylphosphatase-1
- D-3-phosphoglycerate dehydrogenase
- Phosphoglycerate kinase 1
- Glycerate kinase
|
|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5498 |
| Enzyme 1 Name |
Bisphosphoglycerate mutase |
| Enzyme 1 Synonyms |
- 2,3-bisphosphoglycerate mutase, erythrocyte
- 2,3-bisphosphoglycerate synthase
- BPGM
- BPG-dependent PGAM
|
| Enzyme 1 Gene Name |
BPGM |
| Enzyme 1 Protein Sequence |
>Bisphosphoglycerate mutase
MSKYKLIMLRHGEGAWNKENRFCSWVDQKLNSEGMEEARNCGKQLKALNFEFDLVFTSVL
NRSIHTAWLILEELGQEWVPVESSWRLNERHYGALIGLNREQMALNHGEEQVRLWRRSYN
VTPPPIEESHPYYQEIYNDRRYKVCDVPLDQLPRSESLKDVLERLLPYWNERIAPEVLRG
KTILISAHGNSSRALLKHLEGISDEDIINITLPTGVPILLELDENLRAVGPHQFLGDQEA
IQAAIKKVEDQGKVKQAKK
|
| Enzyme 1 Number of Residues |
259 |
| Enzyme 1 Molecular Weight |
30006 |
| Enzyme 1 Theoretical pI |
6.52 |
| Enzyme 1 GO Classification |
| Function |
- catalytic activity
- intramolecular transferase activity
- intramolecular transferase activity, phosphotransferases
- isomerase activity
|
| Process |
- alcohol metabolism
- cellular metabolism
- glucose catabolism
- glucose metabolism
- glycolysis
- hexose metabolism
- metabolism
- monosaccharide metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 1 General Function |
Carbohydrate transport and metabolism |
| Enzyme 1 Specific Function |
Plays a major role in regulating hemoglobin oxygen affinity as a consequence of controlling 2,3-BPG concentration. Can also catalyze the reaction of EC 5.4.2.1 (mutase) and EC 3.1.3.13 (phosphatase), but with a reduced activity |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- 3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
29481  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
P07738  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
PMGE_HUMAN  |
| Enzyme 1 PDB ID |
1T8P  |
| Enzyme 1 PDB File |
Show |
| Enzyme 1 3D Structure |
|
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>780 bp
ATGTCCAAGTACAAACTTATTATGTTAAGACATGGAGAGGGTGCTTGGAATAAGGAGAAC
CGTTTTTGTAGCTGGGTGGATCAGAAACTCAACAGCGAAGGAATGGAGGAAGCTCGGAAC
TGTGGGAAGCAACTCAAAGCGTTAAACTTTGAGTTTGATCTTGTATTCACATCTGTCCTT
AATCGGTCCATTCACACAGCCTGGCTGATCCTGGAAGAGCTAGGCCAGGAATGGGTGCCT
GTGGAAAGCTCCTGGCGTCTAAATGAGCGTCACTATGGGGCCTTGATCGGTCTCAACAGG
GAGCAGATGGCTTTGAATCATGGTGAAGAACAAGTGAGGCTCTGGAGAAGAAGCTACAAT
GTAACCCCGCCTCCCATTGAGGAGTCTCATCCTTACTACCAAGAAATCTACAACGACCGG
AGGTATAAAGTATGCGATGTGCCCTTGGATCAACTGCCACGGTCGGAAAGCTTAAAGGAT
GTTCTGGAGAGACTCCTTCCCTATTGGAATGAAAGGATTGCTCCCGAAGTATTACGTGGC
AAAACCATTCTGATATCTGCTCATGGAAATAGCAGTAGGGCACTCCTAAAACACCTGGAA
GGTATCTCAGATGAAGACATCATCAACATTACTCTTCCTACTGGAGTCCCCATTCTTCTG
GAATTGGATGAAAACCTGCGTGCTGTTGGGCCTCATCAGTTCCTGGGTGACCAAGAGGCG
ATCCAAGCAGCCATTAAGAAAGTAGAAGATCAAGGAAAAGTGAAACAAGCTAAAAAATAG
|
| Enzyme 1 GenBank Gene ID |
X04327  |
| Enzyme 1 GeneCard ID |
BPGM  |
| Enzyme 1 GenAtlas ID |
BPGM  |
| Enzyme 1 HGNC ID |
HGNC:1093  |
| Enzyme 1 Chromosome Location |
7 |
| Enzyme 1 Locus |
7q31-q34 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Joulin V, Peduzzi J, Romeo PH, Rosa R, Valentin C, Dubart A, Lapeyre B, Blouquit Y, Garel MC, Goossens M, et al.: Molecular cloning and sequencing of the human erythrocyte 2,3-bisphosphoglycerate mutase cDNA: revised amino acid sequence. EMBO J. 1986 Sep;5(9):2275-83. [PubMed
]
- Cohen-Solal M, Joulin V, Romeo PH, Rosa R, Valentin C, Garel MC, Rosa J: Molecular cloning of the human 2,3-bisphosphoglycerate mutase cDNA and revised amino acid sequence. Biomed Biochim Acta. 1987;46(2-3):S126-30. [PubMed
]
- Joulin V, Garel MC, Le Boulch P, Valentin C, Rosa R, Rosa J, Cohen-Solal M: Isolation and characterization of the human 2,3-bisphosphoglycerate mutase gene. J Biol Chem. 1988 Oct 25;263(30):15785-90. [PubMed
]
- Stafforini DM, Rollins EN, Prescott SM, McIntyre TM: The platelet-activating factor acetylhydrolase from human erythrocytes. Purification and properties. J Biol Chem. 1993 Feb 25;268(6):3857-65. [PubMed
]
- Craescu CT, Schaad O, Garel MC, Rosa R, Edelstein S: Structural modeling of the human erythrocyte bisphosphoglycerate mutase. Biochimie. 1992 Jun;74(6):519-26. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5501 |
| Enzyme 2 Name |
Phosphoglycerate mutase 1 |
| Enzyme 2 Synonyms |
- Phosphoglycerate mutase isozyme B
- PGAM-B
- BPG-dependent PGAM 1
|
| Enzyme 2 Gene Name |
PGAM1 |
| Enzyme 2 Protein Sequence |
>Phosphoglycerate mutase 1
MAAYKLVLIRHGESAWNLENRFSGWYDADLSPAGHEEAKRGGQALRDAGYEFDICFTSVQ
KRAIRTLWTVLDAIDQMWLPVVRTWRLNERHYGGLTGLNKAETAAKHGEAQVKIWRRSYD
VPPPPMEPDHPFYSNISKDRRYADLTEDQLPSCESLKDTIARALPFWNEEIVPQIKEGKR
VLIAAHGNSLRGIVKHLEGLSEEAIMELNLPTGIPIVYELDKNLKPIKPMQFLGDEETVR
KAMEAVAAQGKAKK
|
| Enzyme 2 Number of Residues |
254 |
| Enzyme 2 Molecular Weight |
28804 |
| Enzyme 2 Theoretical pI |
7.22 |
| Enzyme 2 GO Classification |
| Function |
- catalytic activity
- intramolecular transferase activity
- intramolecular transferase activity, phosphotransferases
- isomerase activity
|
| Process |
- alcohol metabolism
- cellular metabolism
- glucose catabolism
- glucose metabolism
- glycolysis
- hexose metabolism
- metabolism
- monosaccharide metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 2 General Function |
Carbohydrate transport and metabolism |
| Enzyme 2 Specific Function |
Interconversion of 3- and 2-phosphoglycerate with 2,3- bisphosphoglycerate as the primer of the reaction. Can also catalyze the reaction of EC 5.4.2.4 (synthase) and EC 3.1.3.13 (phosphatase), but with a reduced activity |
| Enzyme 2 Pathways |
|
| Enzyme 2 Reactions |
- 3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
551174  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P18669  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
PGAM1_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>765 bp
ATGGCCGCCTACAAACTGGTGCTGATCCGGCACGGCGAGAGCGCATGGAACCTGGAGAAC
CGCTTCAGCGGCTGGTACGACGCCGACCTGAGCCCGGCGGGCCACGAGGAGGCGAAGCGC
GGCGGGCAGGCGCTACGAGATGCTGGCTATGAGTTTGACATCTGCTTCACCTCAGTGCAG
AAGAGAGCGATCCGGACCCTCTGGACAGTGCTAGATGCCATTGATCAGATGTGGCTGCCA
GTGGTGAGGACTTGGCGCCTCAATGAGCGGCACTATGGGGGTCTAACCGGTCTCAATAAA
GCAGAAACTGCTGCAAAGCATGGTGAGGCCCAGGTGAAGATCTGGAGGCGCTCCTATGAT
GTCCCACCACCTCCGATGGAGCCCGACCATCCTTTCTACAGCAACATCAGTAAGGATCGC
AGGTATGCAGACCTCACAGAAGATCAGCTACCCTCCTGTGAGAGTCTGAAGGATACTATT
GCCAGAGCTCTGCCCTTCTGGAATGAAGAAATAGTTCCCCAGATCAAGGAGGGGAAACGT
GTACTGATTGCAGCCCATGGCAACAGCCTCCGGGGCATTGTCAAGCATCTGGAGGGTCTC
TCTGAAGAGGCTATCATGGAGCTGAACCTGCCGACTGGTATTCCCATTGTCTATGAATTG
GACAAGAACTTGAAGCCTATCAAGCCCATGCAGTTTCTGGGGGATGAAGAGACGGTGCGC
AAAGCCATGGAAGCTGTGGCTGCCCAGGGCAAGGCCAAGAAGTGA
|
| Enzyme 2 GenBank Gene ID |
J04173  |
| Enzyme 2 GeneCard ID |
PGAM1  |
| Enzyme 2 GenAtlas ID |
PGAM1  |
| Enzyme 2 HGNC ID |
HGNC:8888  |
| Enzyme 2 Chromosome Location |
10 |
| Enzyme 2 Locus |
10q25.3 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Sakoda S, Shanske S, DiMauro S, Schon EA: Isolation of a cDNA encoding the B isozyme of human phosphoglycerate mutase (PGAM) and characterization of the PGAM gene family. J Biol Chem. 1988 Nov 15;263(32):16899-905. [PubMed
]
- Blouquit Y, Calvin MC, Rosa R, Prome D, Prome JC, Pratbernou F, Cohen-Solal M, Rosa J: Sequence of the human erythrocyte phosphoglycerate mutase by microsequencer and mass spectrometry. J Biol Chem. 1988 Nov 15;263(32):16906-10. [PubMed
]
- Rasmussen RK, Ji H, Eddes JS, Moritz RL, Reid GE, Simpson RJ, Dorow DS: Two-dimensional electrophoretic analysis of human breast carcinoma proteins: mapping of proteins that bind to the SH3 domain of mixed lineage kinase MLK2. Electrophoresis. 1997 Mar-Apr;18(3-4):588-98. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5825 |
| Enzyme 3 Name |
Acylphosphatase-1 |
| Enzyme 3 Synonyms |
- Acylphosphate phosphohydrolase 1
- Acylphosphatase, organ-common type isozyme
- Acylphosphatase, erythrocyte isozyme
|
| Enzyme 3 Gene Name |
ACYP1 |
| Enzyme 3 Protein Sequence |
>Acylphosphatase-1
MAEGNTLISVDYEIFGKVQGVFFRKHTQAEGKKLGLVGWVQNTDRGTVQGQLQGPISKVR
HMQEWLETRGSPKSHIDKANFNNEKVILKLDYSDFQIVK
|
| Enzyme 3 Number of Residues |
99 |
| Enzyme 3 Molecular Weight |
11261 |
| Enzyme 3 Theoretical pI |
9.94 |
| Enzyme 3 GO Classification |
| Function |
- acylphosphatase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on acid anhydrides
- hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 3 General Function |
Energy production and conversion |
| Enzyme 3 Specific Function |
Its physiological role is not yet clear |
| Enzyme 3 Pathways |
|
| Enzyme 3 Reactions |
- An acylphosphate + H2O = a carboxylate + phosphate
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
1834464  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
P07311  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
ACYP1_HUMAN  |
| Enzyme 3 PDB ID |
2ACY  |
| Enzyme 3 PDB File |
Show |
| Enzyme 3 3D Structure |
|
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>300 bp
ATGGCAGAGGGAAACACCCTGATATCAGTGGATTATGAAATTTTTGGGAAGGTGCAAGGG
GTGTTTTTCCGTAAGCATACTCAGGCTGAGGGTAAAAAGCTGGGATTGGTAGGCTGGGTC
CAGAACACTGACCGGGGCACAGTGCAAGGACAATTGCAAGGTCCAATCTCCAAGGTGCGT
CATATGCAGGAATGGCTTGAAACAAGAGGAAGTCCTAAATCACACATCGACAAAGCAAAC
TTCAACAATGAAAAAGTCATCTTGAAGTTGGATTACTCAGACTTCCAAATTGTAAAATAA
|
| Enzyme 3 GenBank Gene ID |
X84194  |
| Enzyme 3 GeneCard ID |
ACYP1  |
| Enzyme 3 GenAtlas ID |
ACYP1  |
| Enzyme 3 HGNC ID |
HGNC:179  |
| Enzyme 3 Chromosome Location |
14 |
| Enzyme 3 Locus |
14q24.3 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed
]
- Liguri G, Camici G, Manao G, Cappugi G, Nassi P, Modesti A, Ramponi G: A new acylphosphatase isoenzyme from human erythrocytes: purification, characterization, and primary structure. Biochemistry. 1986 Dec 2;25(24):8089-94. [PubMed
]
- Fiaschi T, Raugei G, Marzocchini R, Chiarugi P, Cirri P, Ramponi G: Cloning and expression of the cDNA coding for the erythrocyte isoenzyme of human acylphosphatase. FEBS Lett. 1995 Jun 26;367(2):145-8. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
6210 |
| Enzyme 4 Name |
D-3-phosphoglycerate dehydrogenase |
| Enzyme 4 Synonyms |
- 3-PGDH
|
| Enzyme 4 Gene Name |
PHGDH |
| Enzyme 4 Protein Sequence |
>D-3-phosphoglycerate dehydrogenase
MAFANLRKVLISDSLDPCCRKILQDGGLQVVEKQNLSKEELIAELQDCEGLIVRSATKVT
ADVINAAEKLQVVGRAGTGVDNVDLEAATRKGILVMNTPNGNSLSAAELTCGMIMCLARQ
IPQATASMKDGKWERKKFMGTELNGKTLGILGLGRIGREVATRMQSFGMKTIGYDPIISP
EVSASFGVQQLPLEEIWPLCDFITVHTPLLPSTTGLLNDNTFAQCKKGVRVVNCARGGIV
DEGALLRALQSGQCAGAALDVFTEEPPRDRALVDHENVISCPHLGASTKEAQSRCGEEIA
VQFVDMVKGKSLTGVVNAQALTSAFSPHTKPWIGLAEALGTLMRAWAGSPKGTIQVITQG
TSLKNAGNCLSPAVIVGLLKEASKQADVNLVNAKLLVKEAGLNVTTSHSPAAPGEQGFGE
CLLAVALAGAPYQAVGLVQGTTPVLQGLNGAVFRPEVPLRRDLPLLLFRTQTSDPAMLPT
MIGLLAEAGVRLLSYQTSLVSDGETWHVMGISSLLPSLEAWKQHVTEAFQFHF
|
| Enzyme 4 Number of Residues |
533 |
| Enzyme 4 Molecular Weight |
56651 |
| Enzyme 4 Theoretical pI |
6.70 |
| Enzyme 4 GO Classification |
| Function |
- NAD binding
- binding
- catalytic activity
- coenzyme binding
- cofactor binding
- oxidoreductase activity
- oxidoreductase activity, acting on CH-OH group of donors
- oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
- phosphoglycerate dehydrogenase activity
|
| Process |
- L-serine biosynthesis
- L-serine metabolism
- amino acid and derivative metabolism
- amino acid metabolism
- cellular metabolism
- metabolism
- physiological process
- serine family amino acid metabolism
|
| Component |
| — |
|
| Enzyme 4 General Function |
Coenzyme transport and metabolism |
| Enzyme 4 Specific Function |
3-phospho-D-glycerate + NAD(+) = 3- phosphonooxypyruvate + NADH |
| Enzyme 4 Pathways |
- Glycine, Serine and Threonine Metabolism (map00260
)
|
| Enzyme 4 Reactions |
- 3-phosphoglycerate + NAD+ = 3-phosphohydroxypyruvate + NADH + H+
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
2674062  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
O43175  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
SERA_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>1602 bp
ATGGCTTTTGCAAATCTGCGGAAAGTGCTCATCAGTGACAGCCTGGACCCTTGCTGCCGG
AAGATCTTGCAAGAGGGAGGGCTGCAGGTGGTGGAAAAGCAGAACCTTAGCAAAGAGGAG
CTGATAGCGGAGCTGCAGGACTGTGAAGGCCTTATTGTTCGCTCTGCCACCAAGGTGACC
GCTGATGTCATCAACGCAGCTGAGAAACTCCAGGTGGTGGGCAGGGCTGGCACAGGTGTG
GACAATGTGGATCTGGAGGCCGCAACAAGGAAGGGCATCTTGGTTATGAACACCCCCAAT
GGGAACAGCCTCAGTGCCGCAGAACTCACTTGTGGAATGATCATGTGCCTGGCCAGGCAG
ATTCCCCAGGCGACGGCTTCGATGAAGGACGGCAAATGGGAGCGGAAGAAGTTCATGGGA
ACAGAGCTGAATGGAAAGACCCTGGGAATTCTTGGCCTGGGCAGGATTGGGAGAGAGGTA
GCTACCCGGATGCAGTCCTTTGGGATGAAGACTATAGGGTATGACCCCATCATTTCCCCA
GAGGTCTCGGCCTCCTTTGGTGTTCAGCAGCTGCCCCTGGAGGAGATCTGGCCTCTCTGT
GATTTCATCACTGTGCACACTCCTCTCCTGCCCTCCACGACAGGCTTGCTGAATGACAAC
ACCTTTGCCCAGTGCAAGAAGGGGGTGCGTGTGGTGAACTGTGCCCGTGGAGGGATCGTG
GACGAAGGCGCCCTGCTCCGGGCCCTGCAGTCTGGCCAGTGTGCCGGGGCTGCACTGGAC
GTGTTTACGGAAGAGCCGCCACGGGACCGGGCCTTGGTGGACCATGAGAATGTCATCAGC
TGTCCCCACCTGGGTGCCAGCACCAAGGAGGCTCAGAGCCGCTGTGGGGAGGAAATTGCT
GTTCAGTTCGTGGACATGGTGAAGGGGAAATCTCTCACGGGGGTTGTGAATGCCCAGGCC
CTTACCAGTGCCTTCTCTCCACACACCAAGCCTTGGATTGGTCTGGCAGAAGCTCTGGGG
ACACTGATGCGAGCCTGGGCTGGGTCCCCCAAAGGGACCATCCAGGTGATAACACAGGGA
ACATCCCTGAAGAATGCTGGGAACTGCCTAAGCCCCGCAGTCATTGTCGGCCTCCTGAAA
GAGGCTTCCAAGCAGGCGGATGTGAACTTGGTGAACGCTAAGCTGCTGGTGAAAGAGGCT
GGCCTCAATGTCACCACCTCCCACAGCCCTGCTGCACCAGGGGAGCAAGGCTTCGGGGAA
TGCCTCCTGGCCGTGGCCCTGGCAGGCGCCCCTTACCAGGCTGTGGGCTTGGTCCAAGGC
ACTACACCTGTACTGCAGGGGCTCAATGGAGCTGTCTTCAGGCCAGAAGTGCCTCTCCGC
AGGGACCTGCCCCTGCTCCTATTCCGGACTCAGACCTCTGACCCTGCAATGCTGCCTACC
ATGATTGGCCTCCTGGCAGAGGCAGGCGTGCGGCTGCTGTCCTACCAGACTTCACTGGTG
TCAGATGGGGAGACCTGGCACGTCATGGGCATCTCCTCCTTGCTGCCCAGCCTGGAAGCG
TGGAAGCAGCATGTGACTGAAGCCTTCCAGTTCCACTTCTAA
|
| Enzyme 4 GenBank Gene ID |
AF006043  |
| Enzyme 4 GeneCard ID |
PHGDH  |
| Enzyme 4 GenAtlas ID |
PHGDH  |
| Enzyme 4 HGNC ID |
HGNC:8923  |
| Enzyme 4 Chromosome Location |
1 |
| Enzyme 4 Locus |
1p12 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Cho HM, Jun DY, Bae MA, Ahn JD, Kim YH: Nucleotide sequence and differential expression of the human 3-phosphoglycerate dehydrogenase gene. Gene. 2000 Mar 7;245(1):193-201. [PubMed
]
- Klomp LW, de Koning TJ, Malingre HE, van Beurden EA, Brink M, Opdam FL, Duran M, Jaeken J, Pineda M, Van Maldergem L, Poll-The BT, van den Berg IE, Berger R: Molecular characterization of 3-phosphoglycerate dehydrogenase deficiency--a neurometabolic disorder associated with reduced L-serine biosynthesis. Am J Hum Genet. 2000 Dec;67(6):1389-99. Epub 2000 Oct 27. [PubMed
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
6824 |
| Enzyme 5 Name |
Phosphoglycerate kinase 1 |
| Enzyme 5 Synonyms |
- Primer recognition protein 2
- PRP 2
- Cell migration-inducing gene 10 protein
|
| Enzyme 5 Gene Name |
PGK1 |
| Enzyme 5 Protein Sequence |
>Phosphoglycerate kinase 1
MSLSNKLTLDKLDVKGKRVVMRVDFNVPMKNNQITNNQRIKAAVPSIKFCLDNGAKSVVL
MSHLGRPDGVPMPDKYSLEPVAVELKSLLGKDVLFLKDCVGPEVEKACANPAAGSVILLE
NLRFHVEEEGKGKDASGNKVKAEPAKIEAFRASLSKLGDVYVNDAFGTAHRAHSSMVGVN
LPQKAGGFLMKKELNYFAKALESPERPFLAILGGAKVADKIQLINNMLDKVNEMIIGGGM
AFTFLKVLNNMEIGTSLFDEEGAKIVKDLMSKAEKNGVKITLPVDFVTADKFDENAKTGQ
ATVASGIPAGWMGLDCGPESSKKYAEAVTRAKQIVWNGPVGVFEWEAFARGTKALMDEVV
KATSRGCITIIGGGDTATCCAKWNTEDKVSHVSTGGGASLELLEGKVLPGVDALSNI
|
| Enzyme 5 Number of Residues |
417 |
| Enzyme 5 Molecular Weight |
44615 |
| Enzyme 5 Theoretical pI |
8.27 |
| Enzyme 5 GO Classification |
| Function |
- catalytic activity
- kinase activity
- phosphoglycerate kinase activity
- 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 5 General Function |
Carbohydrate transport and metabolism |
| Enzyme 5 Specific Function |
In addition to its role as a glycolytic enzyme, it seems that PGK-1 acts as a polymerase alpha cofactor protein (primer recognition protein) |
| Enzyme 5 Pathways |
|
| Enzyme 5 Reactions |
- ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
35435  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
P00558  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
PGK1_HUMAN  |
| Enzyme 5 PDB ID |
1VJD  |
| Enzyme 5 PDB File |
Show |
| Enzyme 5 3D Structure |
|
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>1254 bp
ATGTCGCTTTCTAACAAGCTGACGCTGGACAAGCTGGACGTTAAAGGGAAGCGGGTCGTT
ATGAGAGTCGACTTCAATGTTCCTATGAAGAACAACCAGATAACAAACAACCAGAGGATT
AAGGCTGCTGTCCCAAGCATCAAATTCTGCTTGGACAATGGAGCCAAGTCGGTAGTCCTT
ATGAGCCACCTAGGCCGGCCTGATGGTGTGCCCATGCCTGACAAGTACTCCTTAGAGCCA
GTTGCTGTAGAACTCAAATCTCTGCTGGGCAAGGATGTTCTGTTCTTGAAGGACTGTGTA
GGCCCAGAAGTGGAGAAAGCCTGTGCCAACCCAGCTGCTGGGTCTGTCATCCTGCTGGAG
AACCTCCGCTTTCATGTGGAGGAAGAAGGGAAGGGAAAAGATGCTTCTGGGAACAAGGTT
AAAGCCGAGCCAGCCAAAATAGAAGCTTTCCGAGCTTCACTTTCCAAGCTAGGGGATGTC
TATGTCAATGATGCTTTTGGCACTGCTCACAGAGCCCACAGCTCCATGGTAGGAGTCAAT
CTGCCACAGAAGGCTGGTGGGTTTTTGATGAAGAAGGAGCTGAACTACTTTGCAAAGGCC
TTGGAGAGCCCAGAGCGACCCTTCCTGGCCATCCTGGGCGGAGCTAAAGTTGCAGACAAG
ATCCAGCTCATCAATAATATGCTGGACAAAGTCAATGAGATGATTATTGGTGGTGGAATG
GCTTTTACCTTCCTTAAGGTGCTCAACAACATGGAGATTGGCACTTCTCTGTTTGATGAA
GAGGGAGCCAAGATTGTCAAAGACCTAATGTCCAAAGCTGAGAAGAATGGTGTGAAGATT
ACCTTGCCTGTTGACTTTGTCACTGCTGACAAGTTTGATGAGAATGCCAAGACTGGCCAA
GCCACTGTGGCTTCTGGCATACCTGCTGGCTGGATGGGCTTGGACTGTGGTCCTGAAAGC
AGCAAGAAGTATGCTGAGGCTGTCACTCGGGCTAAGCAGATTGTGTGGAATGGTCCTGTG
GGGGTATTTGAATGGGAAGCTTTTGCCCGGGGAACCAAAGCTCTCATGGATGAGGTGGTG
AAAGCCACTTCTAGGGGCTGCATCACCATCATAGGTGGTGGAGACACTGCCACTTGCTGT
GCCAAATGGAACACGGAGGATAAAGTCAGCCATGTGAGCACTGGGGGTGGTGCCAGTTTG
GAGCTCCTGGAAGGTAAAGTCCTTCCTGGGGTGGATGCTCTCAGCAATATTTAG
|
| Enzyme 5 GenBank Gene ID |
V00572  |
| Enzyme 5 GeneCard ID |
PGK1  |
| Enzyme 5 GenAtlas ID |
PGK1  |
| Enzyme 5 HGNC ID |
HGNC:8896  |
| Enzyme 5 Chromosome Location |
X |
| Enzyme 5 Locus |
Xq13 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Michelson AM, Markham AF, Orkin SH: Isolation and DNA sequence of a full-length cDNA clone for human X chromosome-encoded phosphoglycerate kinase. Proc Natl Acad Sci U S A. 1983 Jan;80(2):472-6. [PubMed
]
- Michelson AM, Blake CC, Evans ST, Orkin SH: Structure of the human phosphoglycerate kinase gene and the intron-mediated evolution and dispersal of the nucleotide-binding domain. Proc Natl Acad Sci U S A. 1985 Oct;82(20):6965-9. [PubMed
]
- Singer-Sam J, Keith DH, Tani K, Simmer RL, Shively L, Lindsay S, Yoshida A, Riggs AD: Sequence of the promoter region of the gene for human X-linked 3-phosphoglycerate kinase] Gene. 1984 Dec;32(3):409-17. [PubMed
]
- Pfeifer GP, Steigerwald SD, Mueller PR, Wold B, Riggs AD: Genomic sequencing and methylation analysis by ligation mediated PCR. Science. 1989 Nov 10;246(4931):810-3. [PubMed
]
- Huang IY, Welch CD, Yoshida A: Complete amino acid sequence of human phosphoglycerate kinase. Cyanogen bromide peptides and complete amino acid sequence. J Biol Chem. 1980 Jul 10;255(13):6412-20. [PubMed
]
- Jindal HK, Vishwanatha JK: Functional identity of a primer recognition protein as phosphoglycerate kinase. J Biol Chem. 1990 Apr 25;265(12):6540-3. [PubMed
]
- Yoshida A: Hematologically important mutations: molecular abnormalities of phosphoglycerate kinase. Blood Cells Mol Dis. 1996;22(3):265-7. [PubMed
]
- Yoshida A, Twele TW, Dave V, Beutler E: Molecular abnormality of a phosphoglycerate kinase variant (PGK-Alabama). Blood Cells Mol Dis. 1995;21(3):179-81. [PubMed
]
- Cohen-Solal M, Valentin C, Plassa F, Guillemin G, Danze F, Jaisson F, Rosa R: Identification of new mutations in two phosphoglycerate kinase (PGK) variants expressing different clinical syndromes: PGK Creteil and PGK Amiens. Blood. 1994 Aug 1;84(3):898-903. [PubMed
]
- Ookawara T, Dave V, Willems P, Martin JJ, de Barsy T, Matthys E, Yoshida A: Retarded and aberrant splicings caused by single exon mutation in a phosphoglycerate kinase variant. Arch Biochem Biophys. 1996 Mar 1;327(1):35-40. [PubMed
]
- Valentin C, Birgens H, Craescu CT, Brodum-Nielsen K, Cohen-Solal M: A phosphoglycerate kinase mutant (PGK Herlev; D285V) in a Danish patient with isolated chronic hemolytic anemia: mechanism of mutation and structure-function relationships. Hum Mutat. 1998;12(4):280-7. [PubMed
]
- Maeda M, Yoshida A: Molecular defect of a phosphoglycerate kinase variant (PGK-Matsue) associated with hemolytic anemia: Leu----Pro substitution caused by T/A----C/G transition in exon 3. Blood. 1991 Mar 15;77(6):1348-52. [PubMed
]
- Maeda M, Bawle EV, Kulkarni R, Beutler E, Yoshida A: Molecular abnormalities of a phosphoglycerate kinase variant generated by spontaneous mutation. Blood. 1992 May 15;79(10):2759-62. [PubMed
]
- Fujii H, Krietsch WK, Yoshida A: A single amino acid substitution (Asp leads to Asn) in a phosphoglycerate kinase variant (PGK Munchen) associated with enzyme deficiency. J Biol Chem. 1980 Jul 10;255(13):6421-3. [PubMed
]
- Huang IY, Fujii H, Yoshida A: Structure and function of normal and variant human phosphoglycerate kinase. Hemoglobin. 1980;4(5-6):601-9. [PubMed
]
- Fujii H, Kanno H, Hirono A, Shiomura T, Miwa S: A single amino acid substitution (157 Gly----Val) in a phosphoglycerate kinase variant (PGK Shizuoka) associated with chronic hemolysis and myoglobinuria. Blood. 1992 Mar 15;79(6):1582-5. [PubMed
]
- Fujii H, Chen SH, Akatsuka J, Miwa S, Yoshida A: Use of cultured lymphoblastoid cells for the study of abnormal enzymes: molecular abnormality of a phosphoglycerate kinase variant associated with hemolytic anemia. Proc Natl Acad Sci U S A. 1981 Apr;78(4):2587-90. [PubMed
]
- Fujii H, Yoshida A: Molecular abnormality of phosphoglycerate kinase-Uppsala associated with chronic nonspherocytic hemolytic anemia. Proc Natl Acad Sci U S A. 1980 Sep;77(9):5461-5. [PubMed
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
13044 |
| Enzyme 6 Name |
Glycerate kinase |
| Enzyme 6 Synonyms |
- HBeAg-binding protein 4
|
| Enzyme 6 Gene Name |
GLYCTK |
| Enzyme 6 Protein Sequence |
>Glycerate kinase
MAAALQVLPRLARAPLHPLLWRGSVARLASSMALAEQARQLFESAVGAVLPGPMLHRALS
LDPGGRQLKVRDRNFQLRQNLYLVGFGKAVLGMAAAAEELLGQHLVQGVISVPKGIRAAM
ERAGKQEMLLKPHSRVQVFEGAEDNLPDRDALRAALAIQQLAEGLTADDLLLVLISGGGS
ALLPAPIPPVTLEEKQTLTRLLAARGATIQELNTIRKALSQLKGGGLAQAAYPAQVVSLI
LSDVVGDPVEVIASGPTVASSHNVQDCLHILNRYGLRAALPRSVKTVLSRADSDPHGPHT
CGHVLNVIIGSNVLALAEAQRQAEALGYQAVVLSAAMQGDVKSMAQFYGLLAHVARTRLT
PSMAGASVEEDAQLHELAAELQIPDLQLEEALETMAWGRGPVCLLAGGEPTVQLQGSGRG
GRNQELALRVGAELRRWPLGPIDVLFLSGGTDGQDGPTEAAGAWVTPELASQAAAEGLDI
ATFLAHNDSHTFFCCLQGGAHLLHTGMTGTNVMDTHLLFLRPR
|
| Enzyme 6 Number of Residues |
523 |
| Enzyme 6 Molecular Weight |
55253 |
| Enzyme 6 Theoretical pI |
6.72 |
| Enzyme 6 GO Classification |
Not Available |
| Enzyme 6 General Function |
Carbohydrate transport and metabolism |
| Enzyme 6 Specific Function |
ATP + (R)-glycerate = ADP + 3-phospho-(R)- glycerate |
| Enzyme 6 Pathways |
- Glycerolipid Metabolism (map00561
)
- Glycine, Serine and Threonine Metabolism (map00260
)
- Glyoxylate and Dicarboxylate Metabolism (map00630
)
|
| Enzyme 6 Reactions |
- ATP + (R)-glycerate = ADP + 3-phospho-(R)-glycerate [RN:R01514] ALL_REAC R01514
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
31616511  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
Q8IVS8  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
GLCTK_HUMAN  |
| Enzyme 6 PDB ID |
Not Available |
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
Not Available |
| Enzyme 6 GenBank Gene ID |
AY295075  |
| Enzyme 6 GeneCard ID |
Q8IVS8  |
| Enzyme 6 GenAtlas ID |
GLYCTK  |
| Enzyme 6 HGNC ID |
HGNC:24247  |
| Enzyme 6 Chromosome Location |
Not Available |
| Enzyme 6 Locus |
Not Available |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
Not Available |
| Enzyme 6 Metabolite References |
Not Available |