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Human Metabolome Database Version 2.5

 

Showing metabocard for Propionic acid (HMDB00237)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-01-25 11:45:33
Accession Number HMDB00237
Secondary Accession Numbers Not Available
Common Name Propionic acid
Description Propionic acid (PA) is widely used as an antifungal agent in food. It is present naturally at low levels in dairy products and occurs ubiquitously, together with other short-chain fatty acids (SCFA), in the gastro-intestinal tract of humans and other mammals as an end-product of the microbial digestion of carbohydrates. It has significant physiological activity in animals. PA is irritant but produces no acute systemic effects and has no demonstrable genotoxic potential. (PMID 1628870) Propionic aciduria is one of the most frequent organic acidurias, a disease that comprise many various disorders. The outcome of patients born with Propionic aciduria is poor intellectual development patterns, with 60% having an IQ less than 75 and requiring special education. Successful liver and/or renal transplantations, in a few patients, have resulted in better quality of life but have not necessarily prevented neurological and various visceral complications. These results emphasize the need for permanent metabolic follow-up whatever the therapeutic strategy. (PMID 15868474) Decreased early mortality, less severe symptoms at diagnosis, and more favorable short-term neurodevelopmental outcome were recorded in patients identified through expanded newborn screening. (PMID 16763906)
Synonyms
  1. Adofeed
  2. Antischim B
  3. Carboxyethane
  4. Ethanecarboxylate
  5. Ethanecarboxylic acid
  6. Ethylformate
  7. Ethylformic acid
  8. Luprosil
  9. Metacetonate
  10. Metacetonic acid
  11. Methylacetate
  12. Methylacetic acid
  13. MonoProp
  14. Propcorn
  15. Propionate
  16. Propkorn
  17. Prozoin
  18. Pseudoacetate
  19. Pseudoacetic acid
  20. Toxi-Check
  21. Propanoic acid
  22. propanate
  23. Propanoate
Chemical IUPAC Name Propanoic acid
Chemical Formula C3H6O2
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Organic acids
Class
  • Fatty Acids
Sub Class
  • Short chain fatty acids
Family
  • Microbial Metabolite
Species
  • carboxylic acid
Biofunction
Application
Source
  • Endogenous
Average Molecular Weight 74.078
Monoisotopic Molecular Weight 74.036781
Isomeric SMILES CCC(O)=O
Canonical SMILES CCC(O)=O
KEGG Compound ID C00163 Link Image
BioCyc ID PROPIONATE Link Image
BiGG ID 34098 Link Image
Wikipedia Link Propionic acid Link Image
NuGOwiki Link HMDB00237 Link Image
Metagene Link HMDB00237 Link Image
METLIN ID 3215 Link Image
PubChem Compound 1032 Link Image
PubChem Substance 10358066 Link Image
ChEBI ID 30768 Link Image
CAS Registry Number 79-09-4
InChI Identifier InChI=1/C3H6O2/c1-2-3(4)5/h2H2,1H3,(H,4,5)
Synthesis Reference Zhan, Jianghong; Meng, Wei; Gong, Tao; Huang, Fen-sheng. Preparation of propionic acid by propionaldehyde oxidation. Shihua Jishu Yu Yingyong (2005), 23(6), 421-423.
Melting Point (Experimental) -20.7 oC
Experimental Water Solubility 1000.0 mg/mL [US EPA (1981)] Source: PhysProp
Predicted Water Solubility 352.0 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Liquid
Experimental LogP/Hydrophobicity 0.33 [HANSCH,C ET AL. (1995)] Source: PhysProp
Predicted LogP/Hydrophobicity 0.31 [Predicted by ALOGPS]; 0.2 [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 Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Show Image
Show Peaklist
BMRB Spectrum Show Image
Show Peaklist
Cellular Location
  • Cytoplasm
  • Extracellular
  • mitochondria
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Saliva
  • Urine
Tissue Location
Tissue References
Adipose Tissue
Brain
Epidermis
Fibroblasts
Intestine
Muscle
Neuron
Platelet
Stratum Corneum
Testes
Concentrations (Normal)
Biofluid Blood
Value 1.6 +/- 1.2 uM
Age Children:1-13 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 Blood
Value 0.9 +/- 1.2 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 2.8 +/- 3.2 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 Saliva
Value 6420 (5920-6920) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Silwood CJ, Lynch E, Claxson AW, Grootveld MC: 1H and (13)C NMR spectroscopic analysis of human saliva. J Dent Res. 2002 Jun;81(6):422-7. [PubMed Link Image]
Biofluid Urine
Value 2.96 +/- 2.76 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 14.0 (11.4-18.3) umol/mmol creatinine
Age Infant:0-1 yr 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.
Concentrations (Abnormal)
Biofluid Blood
Value 2.5 (0.00-5.00) uM
Age Adult:>18 yrs old
Sex Both
Condition Propionic acidemia
Comments Not Available
References
Associated Disorders
Condition References
Propionic acidemia
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Propanoate Metabolism SMP00016 Link Image map00640 Link Image
General References
  1. Somerma S, Lassus A, Salde L: Assessment of atrophy of human skin caused by corticosteroids using chamber occlusion and suction blister techniques. Acta Derm Venereol. 1984;64(1):41-5. [PubMed Link Image]
  2. Marala RB, Brown JA, Kong JX, Tracey WR, Knight DR, Wester RT, Sun D, Kennedy SP, Hamanaka ES, Ruggeri RB, Hill RJ: Zoniporide: a potent and highly selective inhibitor of human Na(+)/H(+) exchanger-1. Eur J Pharmacol. 2002 Sep 6;451(1):37-41. [PubMed Link Image]
  3. Lin SC, Bergles DE: Synaptic signaling between neurons and glia. Glia. 2004 Aug 15;47(3):290-8. [PubMed Link Image]
  4. Alekseev OM, Widgren EE, Richardson RT, O'Rand MG: Association of NASP with HSP90 in mouse spermatogenic cells: stimulation of ATPase activity and transport of linker histones into nuclei. J Biol Chem. 2005 Jan 28;280(4):2904-11. Epub 2004 Nov 8. [PubMed Link Image]
  5. Robertson MD, Bickerton AS, Dennis AL, Vidal H, Frayn KN: Insulin-sensitizing effects of dietary resistant starch and effects on skeletal muscle and adipose tissue metabolism. Am J Clin Nutr. 2005 Sep;82(3):559-67. [PubMed Link Image]
  6. Esposito BP, Faljoni-Alario A, de Menezes JF, de Brito HF, Najjar R: A circular dichroism and fluorescence quenching study of the interactions between rhodium(II) complexes and human serum albumin. J Inorg Biochem. 1999 May 30;75(1):55-61. [PubMed Link Image]
  7. Jeng JH, Chan CP, Ho YS, Lan WH, Hsieh CC, Chang MC: Effects of butyrate and propionate on the adhesion, growth, cell cycle kinetics, and protein synthesis of cultured human gingival fibroblasts. J Periodontol. 1999 Dec;70(12):1435-42. [PubMed Link Image]
  8. Chandler RJ, Aswani V, Tsai MS, Falk M, Wehrli N, Stabler S, Allen R, Sedensky M, Kazazian HH, Venditti CP: Propionyl-CoA and adenosylcobalamin metabolism in Caenorhabditis elegans: evidence for a role of methylmalonyl-CoA epimerase in intermediary metabolism. Mol Genet Metab. 2006 Sep-Oct;89(1-2):64-73. Epub 2006 Jul 14. [PubMed Link Image]
  9. Silwood CJ, Lynch E, Claxson AW, Grootveld MC: 1H and (13)C NMR spectroscopic analysis of human saliva. J Dent Res. 2002 Jun;81(6):422-7. [PubMed Link Image]
  10. Christensen JK, Varming T, Ahring PK, Jorgensen TD, Nielsen EO: In vitro characterization of 5-carboxyl-2,4-di-benzamidobenzoic acid (NS3763), a noncompetitive antagonist of GLUK5 receptors. J Pharmacol Exp Ther. 2004 Jun;309(3):1003-10. Epub 2004 Feb 25. [PubMed Link Image]
  11. Bintvihok A, Kositcharoenkul S: Effect of dietary calcium propionate on performance, hepatic enzyme activities and aflatoxin residues in broilers fed a diet containing low levels of aflatoxin B1. Toxicon. 2006 Jan;47(1):41-6. Epub 2005 Nov 18. [PubMed Link Image]
  12. Mayer B, Schumacher M, Brandstatter H, Wagner FS, Hermetter A: High-throughput fluorescence screening of antioxidative capacity in human serum. Anal Biochem. 2001 Oct 15;297(2):144-53. [PubMed Link Image]
  13. De Kanter R, De Jager MH, Draaisma AL, Jurva JU, Olinga P, Meijer DK, Groothuis GM: Drug-metabolizing activity of human and rat liver, lung, kidney and intestine slices. Xenobiotica. 2002 May;32(5):349-62. [PubMed Link Image]
  14. Ridge BD, Batt MD, Palmer HE, Jarrett A: The dansyl chloride technique for stratum corneum renewal as an indicator of changes in epidermal mitotic activity following topical treatment. Br J Dermatol. 1988 Feb;118(2):167-74. [PubMed Link Image]
  15. Koeppe RA, Frey KA, Snyder SE, Meyer P, Kilbourn MR, Kuhl DE: Kinetic modeling of N-[11C]methylpiperidin-4-yl propionate: alternatives for analysis of an irreversible positron emission tomography trace for measurement of acetylcholinesterase activity in human brain. J Cereb Blood Flow Metab. 1999 Oct;19(10):1150-63. [PubMed Link Image]
  16. Nguyen TB, Snyder SE, Kilbourn MR: Syntheses of carbon-11 labeled piperidine esters as potential in vivo substrates for acetylcholinesterase. Nucl Med Biol. 1998 Nov;25(8):761-8. [PubMed Link Image]
  17. Wendel U, Zass R, Leupold D: Contribution of odd-numbered fatty acid oxidation to propionate production in neonates with methylmalonic and propionic acidaemias. Eur J Pediatr. 1993 Dec;152(12):1021-3. [PubMed Link Image]
  18. Beutler KT, Pankewycz O, Brautigan DL: Equivalent uptake of organic and inorganic zinc by monkey kidney fibroblasts, human intestinal epithelial cells, or perfused mouse intestine. Biol Trace Elem Res. 1998 Jan;61(1):19-31. [PubMed Link Image]
  19. Wikipedia Link Image
Metabolic Enzymes
  1. Acetyl-coenzyme A synthetase 2-like, mitochondrial precursor
  2. ACSS2 protein
Enzyme 1 [top]
Enzyme 1 ID 5271
Enzyme 1 Name Acetyl-coenzyme A synthetase 2-like, mitochondrial precursor
Enzyme 1 Synonyms
  1. Acetate--CoA ligase 2
  2. Acetyl-CoA synthetase 2
  3. Acyl- CoA synthetase short-chain family member 1
Enzyme 1 Gene Name ACSS1
Enzyme 1 Protein Sequence >Acetyl-coenzyme A synthetase 2-like, mitochondrial precursor
MAARTLGRGVGRLLGSLRGLSGQPARPPCGVSAPRRAASGPSGSAPAVAAAAAQPGSYPA
LSAQAAREPAAFWGPLARDTLVWDTPYHTVWDCDFSTGKIGWFLGGQLNVSVNCLDQHVR
KSPESVALIWERDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVA
AMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGLRGGRVVELKKIVDEAVK
HCPTVQHVLVAHRTDNKVHMGDLDVPLEQEMAKEDPVCAPESMGSEDMLFMLYTSGSTGM
PKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLF
ESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPI
NCEAWEWLHRVVGDSRCTLVDTWWQTETGGICIAPRPSEEGAEILPAMAMRPFFGIVPVL
MDEKGSVVEGSNVSGALCISQAWPGMARTIYGDHQRFVDAYFKAYPGYYFTGDGAYRTEG
GYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKD
SAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQELG
DTTTLEDPSIIAEILSVYQKCKDKQAAAK
Enzyme 1 Number of Residues 689
Enzyme 1 Molecular Weight 74857
Enzyme 1 Theoretical pI 7.11
Enzyme 1 GO Classification
Function
  • AMP binding
  • CoA-ligase activity
  • acetate-CoA ligase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • ligase activity
  • ligase activity, forming carbon-sulfur bonds
  • nucleotide binding
  • purine nucleotide binding
Process
  • metabolism
  • physiological process
Component
Enzyme 1 General Function Lipid transport and metabolism
Enzyme 1 Specific Function Converts acetate to acetyl-CoA so that it can be used for oxidation through the tricarboxylic cycle to produce ATP and CO(2)
Enzyme 1 Pathways
Enzyme 1 Reactions
  • ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-22
Enzyme 1 Transmembrane Regions Not Available
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 56203089 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q9NUB1 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name ACS2L_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1439 bp
CCAAGTGCAAGGTGGTTATCACCTTCAACCAAGGACTCCGGGGTGGGCGCGTGGTGGAGC
TGAAGAAAATAGTGGATGAGGCTGTGAAGCACTGCCCCACCGTGCAGCATGTCCTGGTGG
CTCACAGGACAGACAACAAGGTCCACATGGGGGATCTGGACGTCCCGCTGGAGCAGGAAA
TGGCCAAGGAGGACCCTGTTTGCGCCCCAGAGAGCATGGGCAGTGAGGACATGCTCTTCA
TGCTGTACACCTCAGGGAGCACCGGAATGCCCAAGGGCATCGTCCATACCCAGGCAGGCT
ACCTGCTCTATGCCGCCCTGACTCACAAGCTTGTGTTTGACCACCAGCCAGGTGACATCT
TTGGCTGTGTGGCCGACATCGGTTGGATTACAGGACACAGCTACGTGGTGTATGGGCCTC
TCTGCAATGGTGCCACCAGCGTCCTTTTTGAGAGCACCCCAGTTTATCCCAATGCTGGTC
GGTACTGGGAGACAGTAGAGAGGTTGAAGATCAATCAGTTCTATGGCGCCCCAACGGCTG
TCCGGCTGTTGCTGAAATACGGTGATGCCTGGGTGAAGAAGTATGATCGCTCCTCCCTGC
GGACCCTGGGGTCAGTGGGAGAGCCCATCAACTGTGAGGCCTGGGAGTGGCTTCACAGGG
TGGTGGGGGACAGCAGGTGCACGCTGGTGGACACCTGGTGGCAGACAGAAACAGGTGGCA
TCTGCATCGCACCACGGCCCTCGGAAGAAGGGGCGGAAATCCTCCCTGCCATGGCGATGA
GGCCCTTCTTTGGCATCGTCCCCGTCCTCATGGATGAGAAGGGCAGCGTCGTGGAGGGCA
GCAACGTCTCCGGGGCCCTGTGCATCTCCCAGGCCTGGCCGGGCATGGCCAGGACCATCT
ATGGCGACCACCAGCGATTTGTGGACGCCTACTTCAAGGCCTACCCAGGCTATTACTTCA
CTGGAGACGGGGCTTACCGAACTGAGGGCGGCTATTACCAGATCACAGGGCGGATGGATG
ATGTCATCAACATCAGTGGCCACCGGCTGGGGACCGCAGAGATTGAGGACGCCATCGCCG
ACCACCCTGCAGTACCAGAAAGTGCTGTCATTGGCTACCCCCACGACATCAAAGGAGAAG
CTGCCTTTGCCTTCATTGTGGTGAAAGATAGTGCGGGTGACTCAGATGTGGTGGTGCAGG
AGCTCAAGTCCATGGTGGCCACCAAGATCGCCAAATATGCTGTGCCTGATGAGATCCTGG
TGGTGAAACGTCTTCCAAAAACCAGGTCTGGGAAGGTCATGCGGCGGCTCCTGAGGAAGA
TCATCACTAGTGAGGCCCAGGAGCTGGGAGACACTACCACCTTGGAGGACCCCAGCATCA
TCGCAGAGATCCTGAGTGTCTACCAGAAGTGCAAGGACAAGCAGGCTGCTGCTAAGTGA
Enzyme 1 GenBank Gene ID AL035661 Link Image
Enzyme 1 GeneCard ID ACSS1 Link Image
Enzyme 1 GenAtlas ID ACSS1 Link Image
Enzyme 1 HGNC ID HGNC:16091 Link Image
Enzyme 1 Chromosome Location 20
Enzyme 1 Locus 20p11.23-p11.21
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  2. Nagase T, Nakayama M, Nakajima D, Kikuno R, Ohara O: Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2001 Apr 27;8(2):85-95. [PubMed Link Image]
  3. Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 13088
Enzyme 2 Name ACSS2 protein
Enzyme 2 Synonyms Not Available
Enzyme 2 Gene Name ACSS2
Enzyme 2 Protein Sequence >ACSS2 protein
PMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDAFYRGEKLVNLK
ELADEALQKCQEKGFPVRCCIVVKHLGRAELGMGDSTSQSPPIKRSCPDVQISWNQGIDL
WWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDF
HAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDVNRLWSIVDKYKVTKFY
TAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAQRCPIVDTFWQ
TETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMR
TVYGNHERFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESA
LVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDY
IQNAPGLPKTRSGKIMRRVLRKIAQNDHDLGDMSTVADPSVISHLFSHRCLTIQ
Enzyme 2 Number of Residues 534
Enzyme 2 Molecular Weight 59347
Enzyme 2 Theoretical pI 5.68
Enzyme 2 GO Classification
Function
  • AMP binding
  • CoA-ligase activity
  • acetate-CoA ligase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • ligase activity
  • ligase activity, forming carbon-sulfur bonds
  • nucleotide binding
  • purine nucleotide binding
Process
  • metabolism
  • physiological process
Component
Enzyme 2 General Function Lipid transport and metabolism
Enzyme 2 Specific Function Not Available
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions Not Available
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 40226463 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q96FY7 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name Q96FY7_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence Not Available
Enzyme 2 GenBank Gene ID BC010141 Link Image
Enzyme 2 GeneCard ID Q96FY7 Link Image
Enzyme 2 GenAtlas ID ACSS2 Link Image
Enzyme 2 HGNC ID HGNC:15814 Link Image
Enzyme 2 Chromosome Location Not Available
Enzyme 2 Locus Not Available
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available