EC |
1.2.1.19 |
Accepted name: |
aminobutyraldehyde dehydrogenase |
Reaction: |
4-aminobutanal + NAD+ + H2O = 4-aminobutanoate + NADH + 2 H+ |
|
For diagram of arginine catabolism, click here |
Glossary: |
4-aminobutanoate = γ-aminobutyrate = GABA |
Other name(s): |
γ-guanidinobutyraldehyde dehydrogenase (ambiguous); ABAL dehydrogenase; 4-aminobutyraldehyde dehydrogenase; 4-aminobutanal dehydrogenase; γ-aminobutyraldehyde dehydroganase; 1-pyrroline dehydrogenase; ABALDH; YdcW |
Systematic name: |
4-aminobutanal:NAD+ 1-oxidoreductase |
Comments: |
The enzyme from some species exhibits broad substrate specificity and has a marked preference for straight-chain aldehydes (up to 7 carbon atoms) as substrates [9]. The plant enzyme also acts on 4-guanidinobutanal (cf. EC 1.2.1.54 γ-guanidinobutyraldehyde dehydrogenase). As 1-pyrroline and 4-aminobutanal are in equilibrium and can be interconverted spontaneously, 1-pyrroline may act as the starting substrate. The enzyme forms part of the arginine-catabolism pathway [8] and belongs in the aldehyde dehydrogenase superfamily [9]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9028-98-2 |
References: |
1. |
Callewaert, D.M., Rosemblatt, M.S. and Tchen, T.T. Purification and properties of 4-aminobutanal dehydrogenase from a Pseudomonas species. J. Biol. Chem. 249 (1974) 1737–1741. [PMID: 4817964] |
2. |
Jakoby, W.B. Aldehyde dehydrogenases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 7, Academic Press, New York, 1963, pp. 203–221. |
3. |
Jakoby, W.B. and Fredericks, J. Pyrrolidine and putrescine metabolism: γ-aminobutyraldehyde dehydrogenase. J. Biol. Chem. 234 (1959) 2145–2150. [PMID: 13673029] |
4. |
Matsuda, H. and Suzuki, Y. γ-Guanidinobutyraldehyde dehydrogenase of Vicia faba leaves. Plant Physiol. 76 (1984) 654–657. [PMID: 16663901] |
5. |
Yorifuji, T., Koike, K., Sakurai, T. and Yokoyama, K. 4-Aminobutyraldehyde and 4-guanidinobutyraldehyde dehydrogenases for arginine degradation in Pseudomonas putida. Agric. Biol. Chem. 50 (1986) 2009–2016. |
6. |
Prieto-Santos, M.I., Martin-Checa, J., Balaña-Fouce, R. and Garrido-Pertierra, A. A pathway for putrescine catabolism in Escherichia coli. Biochim. Biophys. Acta 880 (1986) 242–244. [DOI] [PMID: 3510672] |
7. |
Prieto, M.I., Martin, J., Balaña-Fouce, R. and Garrido-Pertierra, A. Properties of γ-aminobutyraldehyde dehydrogenase from Escherichia coli. Biochimie 69 (1987) 1161–1168. [DOI] [PMID: 3129020] |
8. |
Samsonova, N.N., Smirnov, S.V., Novikova, A.E. and Ptitsyn, L.R. Identification of Escherichia coli K12 YdcW protein as a γ-aminobutyraldehyde dehydrogenase. FEBS Lett. 579 (2005) 4107–4112. [DOI] [PMID: 16023116] |
9. |
Gruez, A., Roig-Zamboni, V., Grisel, S., Salomoni, A., Valencia, C., Campanacci, V., Tegoni, M. and Cambillau, C. Crystal structure and kinetics identify Escherichia coli YdcW gene product as a medium-chain aldehyde dehydrogenase. J. Mol. Biol. 343 (2004) 29–41. [DOI] [PMID: 15381418] |
|
[EC 1.2.1.19 created 1965, modified 1989 (EC 1.5.1.35 created 2006, incorporated 2007)] |
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EC
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1.5.1.35
|
Deleted entry: | 1-pyrroline dehydrogenase. The enzyme is identical to EC 1.2.1.19, aminobutyraldehyde dehydrogenase, as the substrates 1-pyrroline and 4-aminobutanal are interconvertible |
[EC 1.5.1.35 created 2006, deleted 2007] |
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|
|
|
EC |
1.5.3.19 |
Accepted name: |
4-methylaminobutanoate oxidase (formaldehyde-forming) |
Reaction: |
4-methylaminobutanoate + O2 + H2O = 4-aminobutanoate + formaldehyde + H2O2 |
|
For diagram of nicotine catabolism by arthrobacter, click here |
Other name(s): |
mabO (gene name) |
Systematic name: |
4-methylaminobutanoate:oxygen oxidoreductase (formaldehyde-forming) |
Comments: |
A flavoprotein (FAD). In the enzyme from the soil bacterium Arthrobacter nicotinovorans the cofactor is covalently bound. Participates in the nicotine degradation pathway of this organism. |
Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc |
References: |
1. |
Chiribau, C.B., Sandu, C., Fraaije, M., Schiltz, E. and Brandsch, R. A novel γ-N-methylaminobutyrate demethylating oxidase involved in catabolism of the tobacco alkaloid nicotine by Arthrobacter nicotinovorans pAO1. Eur. J. Biochem. 271 (2004) 4677–4684. [DOI] [PMID: 15606755] |
|
[EC 1.5.3.19 created 2012] |
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EC |
1.5.3.21 |
Accepted name: |
4-methylaminobutanoate oxidase (methylamine-forming) |
Reaction: |
4-methylaminobutanoate + O2 + H2O = succinate semialdehyde + methylamine + H2O2 |
|
For diagram of nicotine catabolism by arthrobacter, click here |
Other name(s): |
mao (gene name, ambiguous) |
Systematic name: |
4-methylaminobutanoate methylamidohydrolase |
Comments: |
The enzyme participates in the nicotine degradation pathway of the soil bacterium Arthrobacter nicotinovorans. Has a very weak monoamine oxidase (EC 1.4.3.4) activity with 4-aminobutanoate [1]. |
Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Chiribau, C.B., Sandu, C., Fraaije, M., Schiltz, E. and Brandsch, R. A novel γ-N-methylaminobutyrate demethylating oxidase involved in catabolism of the tobacco alkaloid nicotine by Arthrobacter nicotinovorans pAO1. Eur. J. Biochem. 271 (2004) 4677–4684. [DOI] [PMID: 15606755] |
2. |
Chiribau, C.B., Mihasan, M., Ganas, P., Igloi, G.L., Artenie, V. and Brandsch, R. Final steps in the catabolism of nicotine. FEBS J. 273 (2006) 1528–1536. [DOI] [PMID: 16689938] |
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[EC 1.5.3.21 created 2012] |
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EC |
2.6.1.19 |
Accepted name: |
4-aminobutyrate—2-oxoglutarate transaminase |
Reaction: |
4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate |
|
For diagram of arginine catabolism, click here |
Glossary: |
4-aminobutanoate = γ-aminobutyrate = GABA |
Other name(s): |
β-alanine-oxoglutarate transaminase; aminobutyrate aminotransferase (ambiguous); β-alanine aminotransferase; β-alanine-oxoglutarate aminotransferase; γ-aminobutyrate aminotransaminase (ambiguous); γ-aminobutyrate transaminase (ambiguous); γ-aminobutyrate-α-ketoglutarate aminotransferase; γ-aminobutyrate-α-ketoglutarate transaminase; γ-aminobutyrate:α-oxoglutarate aminotransferase; γ-aminobutyric acid aminotransferase (ambiguous); γ-aminobutyric acid transaminase (ambiguous); γ-aminobutyric acid-α-ketoglutarate transaminase; γ-aminobutyric acid-α-ketoglutaric acid aminotransferase; γ-aminobutyric acid-2-oxoglutarate transaminase; γ-aminobutyric transaminase (ambiguous); 4-aminobutyrate aminotransferase (ambiguous); 4-aminobutyrate-2-ketoglutarate aminotransferase; 4-aminobutyrate-2-oxoglutarate aminotransferase; 4-aminobutyrate-2-oxoglutarate transaminase; 4-aminobutyric acid 2-ketoglutaric acid aminotransferase; 4-aminobutyric acid aminotransferase (ambiguous); aminobutyrate transaminase (ambiguous); GABA aminotransferase (ambiguous); GABA transaminase (ambiguous); GABA transferase (ambiguous); GABA-α-ketoglutarate aminotransferase; GABA-α-ketoglutarate transaminase; GABA-α-ketoglutaric acid transaminase; GABA-α-oxoglutarate aminotransferase; GABA-2-oxoglutarate aminotransferase; GABA-2-oxoglutarate transaminase; GABA-oxoglutarate aminotransferase; GABA-oxoglutarate transaminase; glutamate-succinic semialdehyde transaminase; GabT |
Systematic name: |
4-aminobutanoate:2-oxoglutarate aminotransferase |
Comments: |
Requires pyridoxal phosphate. Some preparations also act on β-alanine, 5-aminopentanoate and (R,S)-3-amino-2-methylpropanoate. cf. EC 2.6.1.120, β-alanine—2-oxoglutarate transaminase. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9037-67-6 |
References: |
1. |
Scott, E.M. and Jakoby, W.B. Soluble γ-aminobutyric-glutamic transaminase from Pseudomonas fluorescens. J. Biol. Chem. 234 (1959) 932–936. [PMID: 13654294] |
2. |
Aurich, H. Über die β-Alanin-α-Ketoglutarat-Transaminase aus Neurospora crassa. Hoppe-Seyler's Z. Physiol. Chem. 326 (1961) 25–33. [PMID: 13863304] |
3. |
Schausboe, A., Wu, J.-Y. and Roberts, E. Purification and characterization of the 4-aminobutyrate-2-ketoglutarate transaminase from mouse brain. Biochemistry 12 (1973) 2868–2873. [PMID: 4719123] |
4. |
Bartsch, K., von Johnn-Marteville, A. and Schulz, A. Molecular analysis of two genes of the Escherichia coli gab cluster: nucleotide sequence of the glutamate:succinic semialdehyde transaminase gene (gabT) and characterization of the succinic semialdehyde dehydrogenase gene (gabD). J. Bacteriol. 172 (1990) 7035–7042. [DOI] [PMID: 2254272] |
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[EC 2.6.1.19 created 1965, modified 1982, modified 2012, modified 2021] |
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EC |
2.6.1.96 |
Accepted name: |
4-aminobutyrate—pyruvate transaminase |
Reaction: |
(1) 4-aminobutanoate + pyruvate = succinate semialdehyde + L-alanine (2) 4-aminobutanoate + glyoxylate = succinate semialdehyde + glycine |
Other name(s): |
aminobutyrate aminotransferase (ambiguous); γ-aminobutyrate aminotransaminase (ambiguous); γ-aminobutyrate transaminase (ambiguous); γ-aminobutyric acid aminotransferase (ambiguous); γ-aminobutyric acid pyruvate transaminase; γ-aminobutyric acid transaminase (ambiguous); γ-aminobutyric transaminase (ambiguous); 4-aminobutyrate aminotransferase (ambiguous); 4-aminobutyric acid aminotransferase (ambiguous); aminobutyrate transaminase (ambiguous); GABA aminotransferase (ambiguous); GABA transaminase (ambiguous); GABA transferase (ambiguous); POP2 (gene name) |
Systematic name: |
4-aminobutanoate:pyruvate aminotransferase |
Comments: |
Requires pyridoxal 5′-phosphate. The enzyme is found in plants that do not have the 2-oxoglutarate dependent enzyme (cf. EC 2.6.1.19). The reaction with pyruvate is reversible while the reaction with glyoxylate only takes place in the forward direction. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Van Cauwenberghe, O.R. and Shelp, B.J. Biochemical characterization of partially purified gaba:pyruvate transaminase from Nicotiana tabacum. Phytochemistry 52 (1999) 575–581. |
2. |
Palanivelu, R., Brass, L., Edlund, A.F. and Preuss, D. Pollen tube growth and guidance is regulated by POP2, an Arabidopsis gene that controls GABA levels. Cell 114 (2003) 47–59. [DOI] [PMID: 12859897] |
3. |
Clark, S.M., Di Leo, R., Dhanoa, P.K., Van Cauwenberghe, O.R., Mullen, R.T. and Shelp, B.J. Biochemical characterization, mitochondrial localization, expression, and potential functions for an Arabidopsis γ-aminobutyrate transaminase that utilizes both pyruvate and glyoxylate. J. Exp. Bot. 60 (2009) 1743–1757. [DOI] [PMID: 19264755] |
4. |
Clark, S.M., Di Leo, R., Van Cauwenberghe, O.R., Mullen, R.T. and Shelp, B.J. Subcellular localization and expression of multiple tomato γ-aminobutyrate transaminases that utilize both pyruvate and glyoxylate. J. Exp. Bot. 60 (2009) 3255–3267. [DOI] [PMID: 19470656] |
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[EC 2.6.1.96 created 2012] |
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EC |
3.5.1.63 |
Accepted name: |
4-acetamidobutyrate deacetylase |
Reaction: |
4-acetamidobutanoate + H2O = acetate + 4-aminobutanoate |
Glossary: |
4-aminobutanoate = γ-aminobutyrate = GABA |
Systematic name: |
4-acetamidobutanoate amidohydrolase |
Comments: |
Also acts on N-acetyl-β-alanine and 5-acetamidopentanoate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 102347-82-0 |
References: |
1. |
Haywood, G.W. and Large, P.J. 4-Acetamidobutyrate deacetylase in the yeast Candida boidinii grown on putrescine or spermidine as sole nitrogen source and its probable role in polyamine catabolism. J. Gen. Microbiol. 132 (1986) 7–14. |
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[EC 3.5.1.63 created 1989] |
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EC |
3.5.1.94 |
Accepted name: |
γ-glutamyl-γ-aminobutyrate hydrolase |
Reaction: |
4-(γ-L-glutamylamino)butanoate + H2O = 4-aminobutanoate + L-glutamate |
Glossary: |
4-aminobutanoate = γ-aminobutyrate = GABA |
Other name(s): |
γ-glutamyl-GABA hydrolase; PuuD; YcjL; 4-(γ-glutamylamino)butanoate amidohydrolase; 4-(L-γ-glutamylamino)butanoate amidohydrolase |
Systematic name: |
4-(γ-L-glutamylamino)butanoate amidohydrolase |
Comments: |
Forms part of a putrescine-utilizing pathway in Escherichia coli, in which it has been hypothesized that putrescine is first glutamylated to form γ-glutamylputrescine, which is oxidized to 4-(γ-glutamylamino)butanal and then to 4-(γ-glutamylamino)butanoate. The enzyme can also catalyse the reactions of EC 3.5.1.35 (D-glutaminase) and EC 3.5.1.65 (theanine hydrolase). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Kurihara, S., Oda, S., Kato, K., Kim, H.G., Koyanagi, T., Kumagai, H. and Suzuki, H. A novel putrescine utilization pathway involves γ-glutamylated intermediates of Escherichia coli K-12. J. Biol. Chem. 280 (2005) 4602–4608. [DOI] [PMID: 15590624] |
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[EC 3.5.1.94 created 2006, modified 2011] |
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EC |
3.5.1.125 |
Accepted name: |
N2-acetyl-L-2,4-diaminobutanoate deacetylase |
Reaction: |
(2S)-2-acetamido-4-aminobutanoate + H2O = L-2,4-diaminobutanoate + acetate |
Other name(s): |
doeB (gene name) |
Systematic name: |
(2S)-2-acetamido-4-aminobutanoate amidohydrolase |
Comments: |
The enzyme, found in bacteria, has no activity with (2S)-4-acetamido-2-aminobutanoate (cf. EC 3.5.4.44, ectoine hydrolase). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Schwibbert, K., Marin-Sanguino, A., Bagyan, I., Heidrich, G., Lentzen, G., Seitz, H., Rampp, M., Schuster, S.C., Klenk, H.P., Pfeiffer, F., Oesterhelt, D. and Kunte, H.J. A blueprint of ectoine metabolism from the genome of the industrial producer Halomonas elongata DSM 2581 T. Environ. Microbiol. 13 (2011) 1973–1994. [DOI] [PMID: 20849449] |
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[EC 3.5.1.125 created 2017] |
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EC |
3.5.3.7 |
Accepted name: |
guanidinobutyrase |
Reaction: |
4-guanidinobutanoate + H2O = 4-aminobutanoate + urea |
|
For diagram of arginine catabolism, click here |
Glossary: |
4-aminobutanoate = γ-aminobutyrate = GABA |
Other name(s): |
γ-guanidobutyrase; 4-guanidinobutyrate amidinobutyrase; γ-guanidinobutyrate amidinohydrolase; G-Base; GBH; guanidinobutyrate ureahydrolase |
Systematic name: |
4-guanidinobutanoate amidinohydrolase |
Comments: |
Requires Mn2+. Also acts, very slowly, on 5-guanidinopentanoate and 6-guanidinohexanoate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9013-69-8 |
References: |
1. |
Mora, J., Tarrab, R., Martuscelli, J. and Soberón, G. Characteristics of arginases from ureotelic and non-ureotelic animals. Biochem. J. 96 (1965) 588–594. [PMID: 5862400] |
2. |
Thoai, N.V., Thome-Beau, F. and Olomucki, A. [Induction and specificity of enzymes of the new catabolic arginine pathway] Biochim. Biophys. Acta 115 (1966) 73–80. [DOI] [PMID: 5936244] |
3. |
Yorifuji, T., Kato, M., Kobayashi, T., Ozaki, S. and Ueno, S. 4-Guanidinobutyrate amidinohydrolase from Pseudomonas sp ATCC 14676: purification to homogeneity and properties. Agric. Biol. Chem. 44 (1980) 1127–1134. |
4. |
Yorifuji, T., Kobayashi, T., Tabuchi, A., Shiritani, Y. and Yonaha, K. Distribution of amidinohydrolases among Pseudomonas and comparative studies of some purified enzymes by one-dimensional peptide mapping. Agric. Biol. Chem. 47 (1983) 2825–2830. |
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[EC 3.5.3.7 created 1972] |
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EC |
3.5.4.44 |
Accepted name: |
ectoine hydrolase |
Reaction: |
ectoine + H2O = (2S)-2-acetamido-4-aminobutanoate |
Glossary: |
ectoine = (4S)-2-methyl-1,4,5,6-tetrahydropyrimidine-4-carboxylate |
Other name(s): |
doeA (gene name) |
Systematic name: |
ectoine aminohydrolase |
Comments: |
The enzyme, found in some halophilic bacteria, is involved in the degradation of the compatible solute ectoine. The enzyme, which belongs to peptidase family M24, only acts in the direction of ectoine hydrolysis. It also produces smaller amounts of (2S)-4-acetamido-2-aminobutanoate, which is recycled back to ectoine by EC 4.2.1.108, ectoine synthase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Schwibbert, K., Marin-Sanguino, A., Bagyan, I., Heidrich, G., Lentzen, G., Seitz, H., Rampp, M., Schuster, S.C., Klenk, H.P., Pfeiffer, F., Oesterhelt, D. and Kunte, H.J. A blueprint of ectoine metabolism from the genome of the industrial producer Halomonas elongata DSM 2581 T. Environ. Microbiol. 13 (2011) 1973–1994. [DOI] [PMID: 20849449] |
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[EC 3.5.4.44 created 2017] |
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EC |
4.1.1.15 |
Accepted name: |
glutamate decarboxylase |
Reaction: |
L-glutamate = 4-aminobutanoate + CO2 |
Glossary: |
4-aminobutanoate = γ-aminobutyrate = GABA
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Other name(s): |
L-glutamic acid decarboxylase; L-glutamic decarboxylase; cysteic acid decarboxylase; L-glutamate α-decarboxylase; aspartate 1-decarboxylase; aspartic α-decarboxylase; L-aspartate-α-decarboxylase; γ-glutamate decarboxylase; L-glutamate 1-carboxy-lyase |
Systematic name: |
L-glutamate 1-carboxy-lyase (4-aminobutanoate-forming) |
Comments: |
A pyridoxal-phosphate protein. The brain enzyme also acts on L-cysteate, 3-sulfino-L-alanine and L-aspartate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9024-58-2 |
References: |
1. |
Ambe, L. and Sohonie, K. Purification and properties of glutamate decarboxylase from the field bean (Dolichos lablab). Enzymologia 26 (1963) 98–107. [PMID: 14081858] |
2. |
Nakano, Y. and Kitaoka, S. L-Aspartate α-decarboxylase in a cell-free system from Escherichia coli. J. Biochem. (Tokyo) 70 (1971) 327. [PMID: 4937550] |
3. |
Roberts, E. and Frankel, S. Further studies of glutamic acid decarboxylase in brain. J. Biol. Chem. 190 (1951) 505–512. [PMID: 14841200] |
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[EC 4.1.1.15 created 1961] |
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EC |
6.3.2.11 |
Accepted name: |
carnosine synthase |
Reaction: |
ATP + L-histidine + β-alanine = ADP + phosphate + carnosine |
Glossary: |
carnosine = N-β-alanyl-L-histidine |
Other name(s): |
carnosine synthetase; carnosine-anserine synthetase; homocarnosine-carnosine synthetase; carnosine-homocarnosine synthetase; L-histidine:β-alanine ligase (AMP-forming) (incorrect) |
Systematic name: |
L-histidine:β-alanine ligase (ADP-forming) |
Comments: |
This enzyme was thought to form AMP [1,2], but studies with highly purified enzyme proved that it forms ADP [4]. Carnosine is a dipeptide that is present at high concentrations in skeletal muscle and the olfactory bulb of vertebrates [3]. It is also found in the skeletal muscle of some invertebrates. The enzyme can also catalyse the formation of homocarnosine from 4-aminobutanoate and L-histidine, with much lower activity [4]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9023-61-4 |
References: |
1. |
Kalyankar, G.D. and Meister, A. Enzymatic synthesis of carnosine and related β-alanyl and γ-aminobutyryl peptides. J. Biol. Chem. 234 (1959) 3210–3218. [PMID: 14404206] |
2. |
Stenesh, J.J. and Winnick, T. Carnosine-anserine synthetase of muscle. 4. Partial purification of the enzyme and further studies of β-alanyl peptide synthesis. Biochem. J. 77 (1960) 575–581. [PMID: 16748858] |
3. |
Crush, K.G. Carnosine and related substances in animal tissues. Comp. Biochem. Physiol. 34 (1970) 3–30. [PMID: 4988625] |
4. |
Drozak, J., Veiga-da-Cunha, M., Vertommen, D., Stroobant, V. and Van Schaftingen, E. Molecular identification of carnosine synthase as ATP-grasp domain-containing protein 1 (ATPGD1). J. Biol. Chem. 285 (2010) 9346–9356. [DOI] [PMID: 20097752] |
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[EC 6.3.2.11 created 1965, modified 2010] |
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