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Human Metabolome Database Version 2.5

 

Showing metabocard for Malonic acid (HMDB00691)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2011-06-15 12:35:55
Accession Number HMDB00691
Secondary Accession Numbers Not Available
Common Name Malonic acid
Description Malonic acid (IUPAC systematic name: propanedioic acid) is a dicarboxylic acid with structure CH2(COOH)2. The ionised form of malonic acid, as well as its esters and salts, are known as malonates. For example, diethyl malonate is malonic acid's ethyl ester. The name originates from Latin malum, meaning apple. Malonic acid is the archetypal example of a competitive inhibitor: it acts against succinate dehydrogenase (complex II) in the respiratory electron transport chain.
Synonyms
  1. Propanedioic acid
  2. malonic acid
  3. dicarboxylic acid
  4. Dicarboxymethane
  5. Metahnedicarboxylic acid
  6. Thallium malonate
  7. Dicarboxylate
  8. Propanediolic acid
  9. Kyselina malonova [czech]
  10. Methanedicarboxylic acid
  11. Propanedioic acid dithallium salt
  12. Carboxyacetic acid
  13. Methanedicarbonic acid
  14. Kyselina malonova
  15. Alpha,omega-dicarboxylic acid
  16. Malonate
  17. Malonate dicarboxylic acid
  18. Propanedioate
Chemical IUPAC Name propanedioic acid
Chemical Formula C3H4O4
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Organic acids
Class
  • Dicarboxylic Acids
Sub Class
  • Short chain dicarboxylic acids
Family
  • Mammalian Metabolite
Species
  • carboxylic acid
Biofunction
—
Application
—
Source
  • Endogenous
Average Molecular Weight 104.062
Monoisotopic Molecular Weight 104.010956
Isomeric SMILES OC(=O)CC(O)=O
Canonical SMILES OC(=O)CC(O)=O
KEGG Compound ID C00383 Link Image
BioCyc ID MALONATE Link Image
BiGG ID Not Available
Wikipedia Link Malonic acid Link Image
NuGOwiki Link HMDB00691 Link Image
Metagene Link HMDB00691 Link Image
METLIN ID 3237 Link Image
PubChem Compound 867 Link Image
PubChem Substance 828492 Link Image
ChEBI ID 30794 Link Image
CAS Registry Number 141-82-2
InChI Identifier InChI=1/C3H4O4/c4-2(5)1-3(6)7/h1H2,(H,4,5)(H,6,7)
Synthesis Reference Behr, Arno; Botulinski, Andreas; Carduck, Franz Josef; Schneider, Michael. Process for preparation of malonic acid. Ger. Offen. (1992), 4 pp.
Melting Point (Experimental) 135 oC
Experimental Water Solubility 763.0 mg/mL [YALKOWSKY,SH & DANNENFELSER,RM (1992)] Source: PhysProp
Predicted Water Solubility 197.0 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -2
State Solid
Experimental LogP/Hydrophobicity -0.81 [HANSCH,C ET AL. (1995)] Source: PhysProp
Predicted LogP/Hydrophobicity -0.60 [Predicted by ALOGPS]; -0.3 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID 1NU4 Link Image
Experimental PDB File Show
Experimental PDB Structure
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 Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm (Predicted from LogP)
Biofluid Location
  • Blood
  • Urine
Tissue Location Not Available
Concentrations (Normal)
Biofluid Blood
Value 4.98 +/- 0.31 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Tavazzi B, Lazzarino G, Leone P, Amorini AM, Bellia F, Janson CG, Di Pietro V, Ceccarelli L, Donzelli S, Francis JS, Giardina B: Simultaneous high performance liquid chromatographic separation of purines, pyrimidines, N-acetylated amino acids, and dicarboxylic acids for the chemical diagnosis of inborn errors of metabolism. Clin Biochem. 2005 Nov;38(11):997-1008. Epub 2005 Sep 1. [PubMed Link Image]
Biofluid Blood
Value 15.0+/- 0.58 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Honda A, Yamashita K, Ikegami T, Hara T, Miyazaki T, Hirayama T, Numazawa M, Matsuzaki Y: Highly-sensitive quantification of serum malonate, a possible marker for de novo lipogenesis, by LC-ESI-MS/MS. J Lipid Res. 2009 Apr 29. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid Urine
Value 1.00 (0.00-2.00) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Malonyl-Coa decarboxylase deficiency
Comments Not Available
References
Biofluid Urine
Value 240.00 (40.00-440.00) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Malonyl-Coa decarboxylase deficiency
Comments Not Available
References
Associated Disorders
Condition References
Malonyl-Coa decarboxylase deficiency
OMIM ID
  • 248360 Link Image (Malonyl-Coa decarboxylase deficiency)
Pathways
Name SMPDB Link KEGG Link
Aspartate Metabolism SMP00067 Link Image map00250 Link Image
Fatty Acid Biosynthesis SMP00456 Link Image
General References
  1. Yano S, Sweetman L, Thorburn DR, Mofidi S, Williams JC: A new case of malonyl coenzyme A decarboxylase deficiency presenting with cardiomyopathy. Eur J Pediatr. 1997 May;156(5):382-3. [PubMed Link Image]
  2. Ohdoi C, Nyhan WL, Kuhara T: Chemical diagnosis of Lesch-Nyhan syndrome using gas chromatography-mass spectrometry detection. J Chromatogr B Analyt Technol Biomed Life Sci. 2003 Jul 15;792(1):123-30. [PubMed Link Image]
  3. Belgorodsky B, Fadeev L, Ittah V, Benyamini H, Zelner S, Huppert D, Kotlyar AB, Gozin M: Formation and characterization of stable human serum albumin-tris-malonic acid [C60]fullerene complex. Bioconjug Chem. 2005 Sep-Oct;16(5):1058-62. [PubMed Link Image]
  4. Buyukgebiz B, Jakobs C, Scholte HR, Huijmans JG, Kleijer WJ: Fatal neonatal malonic aciduria. J Inherit Metab Dis. 1998 Feb;21(1):76-7. [PubMed Link Image]
  5. Haan EA, Scholem RD, Croll HB, Brown GK: Malonyl coenzyme A decarboxylase deficiency. Clinical and biochemical findings in a second child with a more severe enzyme defect. Eur J Pediatr. 1986 Apr;144(6):567-70. [PubMed Link Image]
  6. Pollitt RJ, Fowler B, Sardharwalla IB, Edwards MA, Gray RG: Increased excretion of propan-1,3-diol and 3-hydroxypropionic acid apparently caused by abnormal bacterial metabolism in the gut. Clin Chim Acta. 1987 Nov 16;169(2-3):151-7. [PubMed Link Image]
  7. Honda A, Yamashita K, Ikegami T, Hara T, Miyazaki T, Hirayama T, Numazawa M, Matsuzaki Y: Highly-sensitive quantification of serum malonate, a possible marker for de novo lipogenesis, by LC-ESI-MS/MS. J Lipid Res. 2009 Apr 29. [PubMed Link Image]
  8. Wikipedia Link Image
Metabolic Enzymes
  1. 4-aminobutyrate aminotransferase, mitochondrial
  2. cDNA FLJ75643, highly similar to Homo sapiens 4-aminobutyrate aminotransferase
Enzyme 1 [top]
Enzyme 1 ID 5480
Enzyme 1 Name 4-aminobutyrate aminotransferase, mitochondrial
Enzyme 1 Synonyms
  1. (S)-3-amino-2-methylpropionate transaminase
  2. GABA aminotransferase
  3. GABA-AT
  4. Gamma-amino-N-butyrate transaminase
  5. GABA transaminase
  6. GABA-T
  7. L-AIBAT
Enzyme 1 Gene Name ABAT
Enzyme 1 Protein Sequence >4-aminobutyrate aminotransferase, mitochondrial 
MASMLLAQRLACSFQHSYRLLVPGSRHISQAAAKVDVEFDYDGPLMKTEVPGPRSQELMK
QLNIIQNAEAVHFFCNYEESRGNYLVDVDGNRMLDLYSQISSVPIGYSHPALLKLIQQPQ
NASMFVNRPALGILPPENFVEKLRQSLLSVAPKGMSQLITMACGSCSNENALKTIFMWYR
SKERGQRGFSQEELETCMINQAPGCPDYSILSFMGAFHGRTMGCLATTHSKAIHKIDIPS
FDWPIAPFPRLKYPLEEFVKENQQEEARCLEEVEDLIVKYRKKKKTVAGIIVEPIQSEGG
DNHASDDFFRKLRDIARKHGCAFLVDEVQTGGGCTGKFWAHEHWGLDDPADVMTFSKKMM
TGGFFHKEEFRPNAPYRIFNTWLGDPSKNLLLAEVINIIKREDLLNNAAHAGKALLTGLL
DLQARYPQFISRVRGRGTFCSFDTPDDSIRNKLILIARNKGVVLGGCGDKSIRFRPTLVF
RDHHAHLFLNIFSDILADFK
Enzyme 1 Number of Residues 500
Enzyme 1 Molecular Weight 56438.4
Enzyme 1 Theoretical pI 8.04
Enzyme 1 GO Classification
Function
  • 4-aminobutyrate transaminase activity
  • binding
  • catalytic activity
  • cofactor binding
  • pyridoxal phosphate binding
  • transaminase activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid derivative metabolic process
  • cellular metabolic process
  • gamma-aminobutyric acid metabolic process
  • metabolic process
Component
—
Enzyme 1 General Function Involved in 4-aminobutyrate transaminase activity
Enzyme 1 Specific Function Catalyzes the conversion of gamma-aminobutyrate and L- beta-aminoisobutyrate to succinate semialdehyde and methylmalonate semialdehyde, respectively. Can also convert delta-aminovalerate and beta-alanine
Enzyme 1 Pathways
  • Valine, Leucine and Isoleucine Degradation (map00280 Link Image)
Enzyme 1 Reactions
  • (S)-3-amino-2-methylpropanoate + 2-oxoglutarate = 2-methyl-3-oxopropanoate + L-glutamate
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 158254434 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P80404 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name GABT_HUMAN Link Image
Enzyme 1 PDB ID 1OHY Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1503 bp 
ATGGCCTCCATGTTGCTCGCCCAGCGCCTGGCCTGCAGCTTCCAGCACAGCTACCGCCTG
CTGGTGCCTGGATCCAGACACATTAGTCAAGCTGCAGCCAAAGTCGACGTTGAATTTGAT
TATGATGGGCCTCTGATGAAGACGGAAGTCCCAGGGCCTAGATCTCAGGAGTTAATGAAA
CAGCTGAATATAATTCAGAATGCAGAGGCTGTGCATTTTTTCTGCAATTACGAAGAGAGC
CGAGGCAATTACCTGGTTGATGTGGACGGCAACCGAATGCTGGATCTTTATTCCCAGATC
TCCTCTGTTCCCATAGGTTACAGCCACCCCGCCCTGCTGAAACTCATCCAACAGCCTCAA
AATGCGAGCATGTTTGTCAACAGACCCGCCCTCGGAATCCTGCCTCCGGAGAACTTTGTG
GAGAAGCTCCGGCAGTCCTTGCTCTCGGTGGCTCCCAAAGGGATGTCCCAGCTCATCACC
ATGGCCTGCGGCTCCTGCTCCAATGAAAACGCCTTAAAGACCATCTTCATGTGGTACCGG
AGCAAGGAAAGAGGGCAGAGGGGCTTCTCCCAGGAGGAGCTGGAGACGTGCATGATTAAC
CAGGCCCCTGGCTGCCCCGACTACAGCATCCTCTCCTTCATGGGCGCGTTCCATGGGAGG
ACCATGGGTTGCTTAGCGACCACGCACTCTAAAGCCATTCACAAGATCGACATCCCTTCC
TTTGACTGGCCCATCGCACCGTTCCCACGGCTGAAATACCCTCTGGAAGAGTTTGTGAAA
GAGAACCAACAGGAGGAGGCCCGCTGTCTGGAAGAGGTGGAGGATCTGATTGTGAAATAT
CGGAAAAAGAAGAAGACGGTGGCCGGGATCATCGTGGAGCCCATCCAGTCCGAGGGTGGA
GACAACCACGCATCCGATGACTTCTTTCGGAAGCTGAGAGACATCGCCAGGAAGCATGGC
TGCGCCTTCTTGGTGGACGAGGTACAGACCGGAGGAGGCTGCACGGGCAAGTTCTGGGCC
CATGAGCACTGGGGCCTGGATGACCCAGCAGACGTGATGACCTTCAGCAAGAAGATGATG
ACTGGGGGCTTCTTCCACAAGGAGGAGTTCAGGCCTAATGCTCCCTACCGGATCTTCAAC
ACCTGGCTGGGGGACCCGTCCAAGAACCTGTTGCTGGCTGAGGTCATCAACATCATCAAG
CGGGAGGACCTGCTAAATAATGCAGCCCATGCCGGGAAGGCCCTGCTCACAGGACTGCTG
GACCTCCAGGCCCGGTACCCCCAGTTCATCAGCAGGGTGAGAGGACGAGGCACCTTTTGC
TCCTTCGATACTCCCGATGATTCCATACGGAATAAGCTCATTTTAATTGCCAGAAACAAA
GGTGTGGTGTTGGGTGGCTGTGGTGACAAATCCATTCGTTTCCGTCCCACGCTGGTCTTC
AGGGATCACCACGCTCACCTGTTCCTCAATATTTTCAGTGACATCTTAGCAGACTTCAAG
TAA
Enzyme 1 GenBank Gene ID AK290501 Link Image
Enzyme 1 GeneCard ID ABAT Link Image
Enzyme 1 GenAtlas ID ABAT Link Image
Enzyme 1 HGNC ID HGNC:23 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 16p13.2
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Osei YD, Churchich JE: Screening and sequence determination of a cDNA encoding the human brain 4-aminobutyrate aminotransferase. Gene. 1995 Apr 3;155(2):185-7. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. De Biase D, Barra D, Simmaco M, John RA, Bossa F: Primary structure and tissue distribution of human 4-aminobutyrate aminotransferase. Eur J Biochem. 1995 Jan 15;227(1-2):476-80. [PubMed Link Image]
  5. Medina-Kauwe LK, Tobin AJ, De Meirleir L, Jaeken J, Jakobs C, Nyhan WL, Gibson KM: 4-Aminobutyrate aminotransferase (GABA-transaminase) deficiency. J Inherit Metab Dis. 1999 Jun;22(4):414-27. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 12979
Enzyme 2 Name cDNA FLJ75643, highly similar to Homo sapiens 4-aminobutyrate aminotransferase
Enzyme 2 Synonyms
  1. ABAT, nuclear gene encoding mitochondrial protein, transcript variant 2, mRNA
Enzyme 2 Gene Name Not Available
Enzyme 2 Protein Sequence >cDNA FLJ75643, highly similar to Homo sapiens 4-aminobutyrate aminotransferase 
MASMLLAQRLACSFQHSYRLLVPGSRHISQAAAKVDVEFDYDGPLMKTEVPGPRSQELMK
QLNIIQNAEAVHFFCNYEESRGNYLVDVDGNRMLDLYSQISSVPIGYSHPALLKLIQQPQ
NASMFVNRPALGILPPENFVEKLRQSLLSVAPKGMSQLITMACGSCSNENALKTIFMWYR
SKERGQRGFSQEELETCMINQAPGCPDYSILSFMGAFHGRTMGCLATTHSKAIHKIDIPS
FDWPIAPFPRLKYPLEEFVKENQQEEARCLEEVEDLIVKYRKKKKTVAGIIVEPIQSEGG
DNHASDDFFRKLRDIARKHGCAFLVDEVQTGGGCTGKFWAHEHWGLDDPADVMTFSKKMM
TGGFFHKEEFRPNAPYRIFNTWLGDPSKNLLLAEVINIIKREDLLNNAAHAGKALLTGLL
DLQARYPQFISRVRGRGTFCSFDTPDDSIRNKLILIARNKGVVLGGCGDKSIRFRPTLVF
RDHHAHLFLNIFSDILADFK
Enzyme 2 Number of Residues 500
Enzyme 2 Molecular Weight 56440
Enzyme 2 Theoretical pI 8.04
Enzyme 2 GO Classification Not Available
Enzyme 2 General Function Amino acid transport and metabolism
Enzyme 2 Specific Function Not Available
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions Not Available
Enzyme 2 Pfam Domain Function Not Available
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 158254434 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID A8K386 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name A8K386_HUMAN Link Image
Enzyme 2 PDB ID 1OHY Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence Not Available
Enzyme 2 GenBank Gene ID AK290501 Link Image
Enzyme 2 GeneCard ID A8K386 Link Image
Enzyme 2 GenAtlas ID Not Available
Enzyme 2 HGNC ID Not Available
Enzyme 2 Chromosome Location Not Available
Enzyme 2 Locus Not Available
Enzyme 2 SNPs Not Available
Enzyme 2 General References Not Available
Enzyme 2 Metabolite References Not Available