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Human Metabolome Database Version 2.5

 

Showing metabocard for (S)-b-aminoisobutyric acid (HMDB02166)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2006-05-22 15:17:39
Update Date 2009-05-05 20:59:08
Accession Number HMDB02166
Secondary Accession Numbers Not Available
Common Name (S)-b-aminoisobutyric acid
Description Beta-Aminoisobutyric acid is a non-protein amino acid originating from the catabolism of thymine and valine. The concentration of beta-Aminoisobutyric acid is normally low in urine as beta-Aminoisobutyric acid is further catabolized by b-aminoisobutyrate aminotransferases to methylmalonic acid semialdehyde and propionyl-CoA. beta-Aminoisobutyric acid occurs in two isomeric forms and both enantiomers of beta-Aminoisobutyric acid can be detected in human urine and plasma. In plasma, the S-enantiomer is the predominant type due to active renal reabsorption. In contrast, urine almost exclusively contains the R-enantiomer of beta-Aminoisobutyric acid, which is eliminated both by filtration and tubular secretion. Persistently increased levels of beta-Aminoisobutyric acid have been observed in individuals with a deficiency of R (-) -b-aminoisobutyrate-pyruvate aminotransferase. In addition, transient high levels of beta-Aminoisobutyric acid have been observed under a variety of pathological conditions such as lead poisoning, starvation, in total body irradiation and in a number of malignancies. The S-enantiomer of beta-Aminoisobutyric acid is predominantly derived from the catabolism of valine. It has been suggested that an altered homoeostasis of b-alanine underlies some of the clinical abnormalities encountered in patients with a dihydropyrimidine dehydrogenase (DPD) deficiency. DPD constitutes the first step of the pyrimidine degradation pathway, in which the pyrimidine bases uracil and thymine are catabolized to b-alanine and the R-enantiomer of beta-Aminoisobutyric acid respectively. In normal individuals with an intact pyrimidine degradation pathway, R-methylmalonic acid semialdehyde can be synthesized directly from the catabolism of thymine. Hence, there might be less cross-over between the valine and thymine pathway, allowing the conversion of S-methylmalonic acid semialdehyde into S-beta-Aminoisobutyric acid and the subsequent accumulation of S-beta-Aminoisobutyric acid in plasma. (PMID: 14705962, 14292857, 14453202)
Synonyms
  1. L-b-Aminoisobutyric acid
  2. L-3-Amino-2-methylpropionic acid
  3. L-3-Amino-2-methylpropanoic acid
  4. L-2-methyl-b-Alanine
  5. (S)-b-Aminoisobutyric acid
  6. (S)-3-amino-2-methyl-Propanoic acid
  7. (+)-b-Aminoisobutyric acid
  8. (+)-a-Methyl-b-alanine
  9. S-b-aminoisobutyrate
  10. S-beta-aminoisobutyrate
  11. S-beta-aminoisobutyric acid
  12. L-beta-Aminoisobutyric acid
  13. L-2-methyl-beta-Alanine
  14. (S)-beta-Aminoisobutyric acid
  15. (+)-beta-Aminoisobutyric acid
  16. (+)-alpha-Methyl-beta-alanine
  17. L-beta-aminoisobutyrate
  18. L-b-aminoisobutyrate
  19. L-3-Amino-isobutanoate
  20. (S)-3-Amino-isobutyrate
  21. L-3-Amino-isobutyrate
  22. (S)-3-Amino-isobutanoate
  23. (S)-3-Amino-2-methylpropanoate
  24. L-3-Amino-isobutanoic acid
  25. (S)-3-Amino-isobutyric acid
  26. L-3-Amino-isobutyric acid
  27. (S)-3-Amino-isobutanoic acid
  28. (S)-3-Amino-2-methylpropanoic acid
  29. L-3-Amino-2-methylpropanoate
  30. (S)-3-amino-2-methyl-Propanoate
Chemical IUPAC Name (2S)-3-amino-2-methylpropanoic acid
Chemical Formula C4H9NO2
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Amino acids and Amino Acid conjugates
Class
  • Amino Acids
Sub Class
  • NA
Family
  • Mammalian Metabolite
Species
  • primary amine
  • primary aliphatic amine (alkylamine)
  • carboxylic acid
Biofunction
  • Protein synthesis, amino acid biosynthesis
Application
—
Source
  • Endogenous
Average Molecular Weight 103.120
Monoisotopic Molecular Weight 103.063332
Isomeric SMILES C[C@@H](CN)C(O)=O
Canonical SMILES CC(CN)C(O)=O
KEGG Compound ID C03284 Link Image
BioCyc ID Not Available
BiGG ID Not Available
Wikipedia Link Not Available
NuGOwiki Link HMDB02166 Link Image
Metagene Link HMDB02166 Link Image
METLIN ID 6520 Link Image
PubChem Compound 439434 Link Image
PubChem Substance 15486482 Link Image
ChEBI ID 33094 Link Image
CAS Registry Number 4249-19-8
InChI Identifier InChI=1/C4H9NO2/c1-3(2-5)4(6)7/h3H,2,5H2,1H3,(H,6,7)/t3-/m0/s1
Synthesis Reference Alauddin, Mian M.; Fissekis, John D.; Conti, Peter S. a-Alkylation of amino acid derivatives: synthesis and chiral resolution of [11C]b-aminoisobutyric acid. Nuclear Medicine and Biology (1997), 24(8), 771-775.
Melting Point (Experimental) 175-177 oC
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 367.0 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -2.97 [Predicted by ALOGPS] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location Not Available
Biofluid Location
  • Blood
  • Urine
Tissue Location Not Available
Concentrations (Normal)
Biofluid Blood
Value 1.03 +/- 0.34 uM
Age Adult:>18 yrs old
Sex Male
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 Urine
Value 7.0 +/- 6.6 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Female
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 Urine
Value 10.0 +/- 9.0 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by Cornelius Lentner.
  • West Cadwell, N.J. : Medical education Div., Ciba-Geigy Corp.
  • Basel, Switzerland c1981-1992.
Biofluid Urine
Value 4.3 +/- 2.9 umol/mmol creatinine
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 Cornelius Lentner.
  • West Cadwell, N.J. : Medical education Div., Ciba-Geigy Corp.
  • Basel, Switzerland c1981-1992.
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Valine, Leucine and Isoleucine Degradation SMP00032 Link Image map00280 Link Image
General References
  1. Roe CR, Struys E, Kok RM, Roe DS, Harris RA, Jakobs C: Methylmalonic semialdehyde dehydrogenase deficiency: psychomotor delay and methylmalonic aciduria without metabolic decompensation. Mol Genet Metab. 1998 Sep;65(1):35-43. [PubMed Link Image]
Metabolic Enzymes
  1. 4-aminobutyrate aminotransferase, mitochondrial
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