EC |
1.4.1.25 |
Accepted name: |
L-arginine dehydrogenase |
Reaction: |
L-arginine + H2O + NAD(P)+ = 5-guanidino-2-oxopentanoate + NH3 + NAD(P)H + H+ |
Other name(s): |
dauB (gene name); anabolic L-arginine dehydrogenase |
Systematic name: |
L-arginine:NAD(P)+ oxidoreductase (deaminating) |
Comments: |
The enzyme, which has been isolated from the bacterium Pseudomonas aeruginosa PAO1, forms with EC 1.4.99.6, D-arginine dehydrogenase, a two-enzyme complex involved in the racemization of D- and L-arginine. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Li, C. and Lu, C.D. Arginine racemization by coupled catabolic and anabolic dehydrogenases. Proc. Natl. Acad. Sci. USA 106 (2009) 906–911. [DOI] [PMID: 19139398] |
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[EC 1.4.1.25 created 2017] |
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EC |
1.4.3.25 |
Accepted name: |
L-arginine oxidase |
Reaction: |
L-arginine + H2O + O2 = 5-guanidino-2-oxopentanoate + NH3 + H2O2 |
Systematic name: |
L-arginine:oxygen oxidoreductase (deaminating) |
Comments: |
Contains FAD. The enzyme from cyanobacteria can also act on other basic amino acids with lower activity. The enzyme from the bacterium Pseudomonas sp. TPU 7192 is highly specific. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Miller, D.L. and Rodwell, V.W. Metabolism of basic amino acids in Pseudomonas putida. Intermediates in L-arginine catabolism. J. Biol. Chem. 246 (1971) 5053–5058. [PMID: 5570437] |
2. |
Pistorius, E.K. and Voss, H. Some properties of a basic L-amino-acid oxidase from Anacystis nidulans. Biochim. Biophys. Acta 611 (1980) 227–240. [DOI] [PMID: 6766743] |
3. |
Gau, A.E., Heindl, A., Nodop, A., Kahmann, U. and Pistorius, E.K. L-Amino acid oxidases with specificity for basic L-amino acids in cyanobacteria. Z. Naturforsch. C 62 (2007) 273–284. [PMID: 17542496] |
4. |
Matsui, D., Terai, A. and Asano, Y. L-Arginine oxidase from Pseudomonas sp. TPU 7192: Characterization, gene cloning, heterologous expression, and application to L-arginine determination. Enzyme Microb. Technol. 82 (2016) 151–157. [DOI] [PMID: 26672462] |
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[EC 1.4.3.25 created 2017] |
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EC |
1.4.99.6 |
Accepted name: |
D-arginine dehydrogenase |
Reaction: |
D-arginine + acceptor + H2O = 5-guanidino-2-oxopentanoate + NH3 + reduced acceptor (overall reaction) (1a) D-arginine + acceptor = iminoarginine + reduced acceptor (1b) iminoarginine + H2O = 5-guanidino-2-oxopentanoate + NH3 (spontaneous) |
Glossary: |
5-guanidino-2-oxopentanoate = 2-ketoarginine
iminoarginine = 5-carbamimidamido-2-iminopentanoate |
Other name(s): |
D-amino-acid:(acceptor) oxidoreductase (deaminating); D-amino-acid dehydrogenase; D-amino-acid:acceptor oxidoreductase (deaminating) |
Systematic name: |
D-arginine:acceptor oxidoreductase (deaminating) |
Comments: |
Contains a non-covalent FAD cofactor. The enzyme, which has been isolated from the bacterium Pseudomonas aeruginosa PAO1, forms with EC 1.4.1.25, L-arginine dehydrogenase, a two-enzyme complex involved in the racemization of D- and L-arginine. The enzyme has a broad substrate range and can act on most D-amino acids with the exception of D-glutamate and D-aspartate. However, activity is maximal with D-arginine and D-lysine. Not active on glycine. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37205-44-0 |
References: |
1. |
Tsukada, K. D-Amino acid dehydrogenases of Pseudomonas fluorescens. J. Biol. Chem. 241 (1966) 4522–4528. [PMID: 5925166] |
2. |
Li, C. and Lu, C.D. Arginine racemization by coupled catabolic and anabolic dehydrogenases. Proc. Natl. Acad. Sci. USA 106 (2009) 906–911. [DOI] [PMID: 19139398] |
3. |
Fu, G., Yuan, H., Li, C., Lu, C.D., Gadda, G. and Weber, I.T. Conformational changes and substrate recognition in Pseudomonas aeruginosa D-arginine dehydrogenase. Biochemistry 49 (2010) 8535–8545. [DOI] [PMID: 20809650] |
4. |
Yuan, H., Fu, G., Brooks, P.T., Weber, I. and Gadda, G. Steady-state kinetic mechanism and reductive half-reaction of D-arginine dehydrogenase from Pseudomonas aeruginosa. Biochemistry 49 (2010) 9542–9550. [DOI] [PMID: 20932054] |
5. |
Fu, G., Yuan, H., Wang, S., Gadda, G. and Weber, I.T. Atomic-resolution structure of an N5 flavin adduct in D-arginine dehydrogenase. Biochemistry 50 (2011) 6292–6294. [DOI] [PMID: 21707047] |
6. |
Yuan, H., Xin, Y., Hamelberg, D. and Gadda, G. Insights on the mechanism of amine oxidation catalyzed by D-arginine dehydrogenase through pH and kinetic isotope effects. J. Am. Chem. Soc. 133 (2011) 18957–18965. [DOI] [PMID: 21999550] |
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[EC 1.4.99.6 created 1972 as EC 1.4.99.1, transferred 2015 to EC 1.4.99.6, modified 2017] |
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EC |
2.1.1.243 |
Accepted name: |
2-ketoarginine methyltransferase |
Reaction: |
S-adenosyl-L-methionine + 5-guanidino-2-oxopentanoate = S-adenosyl-L-homocysteine + 5-guanidino-3-methyl-2-oxopentanoate |
Glossary: |
5-guanidino-2-oxopentanoate = 2-ketoarginine
5-guanidino-3-methyl-2-oxopentanoate = 5-carbamimidamido-3-methyl-2-oxopentanoate |
Other name(s): |
mrsA (gene name) |
Systematic name: |
S-adenosyl-L-methionine:5-carbamimidamido-2-oxopentanoate S-methyltransferase |
Comments: |
The enzyme is involved in production of the rare amino acid 3-methylarginine, which is used by the epiphytic bacterium Pseudomonas syringae pv. syringae as an antibiotic against the related pathogenic species Pseudomonas syringae pv. glycinea. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Braun, S.D., Hofmann, J., Wensing, A., Ullrich, M.S., Weingart, H., Völksch, B. and Spiteller, D. Identification of the biosynthetic gene cluster for 3-methylarginine, a toxin produced by Pseudomonas syringae pv. syringae 22d/93. Appl. Environ. Microbiol. 76 (2010) 2500–2508. [DOI] [PMID: 20190091] |
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[EC 2.1.1.243 created 2012] |
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EC |
2.6.1.84 |
Accepted name: |
arginine—pyruvate transaminase |
Reaction: |
L-arginine + pyruvate = 5-guanidino-2-oxopentanoate + L-alanine |
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For diagram of arginine-catabolism pathway, click here |
Other name(s): |
arginine:pyruvate transaminase; AruH; ATase |
Systematic name: |
L-arginine:pyruvate aminotransferase |
Comments: |
A pyridoxal-phosphate protein. While L-arginine is the best substrate, the enzyme exhibits broad substrate specificity, with L-lysine, L-methionine, L-leucine, L-ornithine and L-glutamine also able to act as substrates, but more slowly. Pyruvate cannot be replaced by 2-oxoglutarate as amino-group acceptor. This is the first catalytic enzyme of the arginine transaminase pathway for L-arginine utilization in Pseudomonas aeruginosa. This pathway is only used when the major route of arginine catabolism, i.e. the arginine succinyltransferase pathway, is blocked. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Yang, Z. and Lu, C.-D. Characterization of an arginine:pyruvate transaminase in arginine catabolism of Pseudomonas aeruginosa PAO1. J. Bacteriol. 189 (2007) 3954–3959. [DOI] [PMID: 17416668] |
2. |
Yang, Z. and Lu, C.D. Functional genomics enables identification of genes of the arginine transaminase pathway in Pseudomonas aeruginosa. J. Bacteriol. 189 (2007) 3945–3953. [DOI] [PMID: 17416670] |
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[EC 2.6.1.84 created 2007] |
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EC |
4.1.1.75 |
Accepted name: |
5-guanidino-2-oxopentanoate decarboxylase |
Reaction: |
5-guanidino-2-oxopentanoate = 4-guanidinobutanal + CO2 |
Glossary: |
thiamine diphosphate = 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-(2-diphosphoethyl)-4-methyl-1,3-thiazolium |
Other name(s): |
α-ketoarginine decarboxylase; 2-oxo-5-guanidinopentanoate carboxy-lyase |
Systematic name: |
5-guanidino-2-oxopentanoate carboxy-lyase (4-guanidinobutanal-forming) |
Comments: |
Enzyme activity is dependent on the presence of thiamine diphosphate and a divalent cation. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 56831-67-5 |
References: |
1. |
Vanderbilt, A.S., Gaby, N.S., Rodwell, V.W. Intermediates and enzymes between α-ketoarginine and γ-guanidinobutyrate in the L-arginine catabolic pathway of Pseudomonas putida. J. Biol. Chem. 250 (1975) 5322–5329. [PMID: 237915] |
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[EC 4.1.1.75 created 1999] |
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