| EC |
2.1.1.243 |
| Accepted name: |
5-guanidino-2-oxopentanoate (3R)-methyltransferase |
| Reaction: |
S-adenosyl-L-methionine + 5-guanidino-2-oxopentanoate = S-adenosyl-L-homocysteine + (3R)-5-guanidino-3-methyl-2-oxopentanoate |
| Glossary: |
5-guanidino-2-oxopentanoate = 2-ketoarginine
(3R)-5-guanidino-3-methyl-2-oxopentanoate = (3R)-5-carbamimidamido-3-methyl-2-oxopentanoate |
| Other name(s): |
mrsA (gene name); argN (gene name); 2-ketoarginine methyltransferase; S-adenosyl-L-methionine:5-carbamimidamido-2-oxopentanoate S-methyltransferase |
| Systematic name: |
S-adenosyl-L-methionine:5-guanidino-2-oxopentanoate (3R)-methyltransferase |
| Comments: |
The enzyme is involved in production of the rare amino acid (3R)-3-methyl-L-arginine. The compound is used by the epiphytic bacterium Pseudomonas syringae pv. syringae as an antibiotic against the related pathogenic species Pseudomonas savastanoi pv. glycinea. Other bacteria incorporate the compound into more complex compounds such as the peptidyl nucleoside antibiotic arginomycin. |
| 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] |
| 2. |
Feng, J., Wu, J., Gao, J., Xia, Z., Deng, Z. and He, X. Biosynthesis of the β-methylarginine residue of peptidyl nucleoside arginomycin in Streptomyces arginensis NRRL 15941. Appl. Environ. Microbiol. 80 (2014) 5021–5027. [DOI] [PMID: 24907335] |
|
| [EC 2.1.1.243 created 2012, modified 2024] |
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| EC |
2.6.1.125 |
| Accepted name: |
L-arginine:2-oxoglutarate transaminase |
| Reaction: |
L-arginine + 2-oxoglutarate = 5-guanidino-2-oxopentanoate + L-glutamate |
| Other name(s): |
argM (gene name); arginine-α-ketoglutarate transaminase |
| Systematic name: |
L-arginine:2-oxoglutarate aminotransferase |
| Comments: |
Requires pyridoxal 5′-phosphate. The enzyme, characterized from several bacterial species, is known to participate in L-arginine degradation and in the biosynthesis of the rare amino acid (3R)-3-methyl-L-arginine. The enzyme from Streptomyces arginensis also catalyses the activity of EC 2.6.1.126, L-aspartate:5-guanidino-3-methyl-2-oxopentanoate transaminase. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Tachiki, T., Kohno, H., Sugiyama, K., Matsubara, T. and Tochikura, T. Purification, properties and formation of arginine-α-ketoglutarate transaminase in Arthrobacter simplex. Biochim. Biophys Acta 615 (1980) 79–84. [DOI] [PMID: 7426667] |
| 2. |
Feng, J., Wu, J., Gao, J., Xia, Z., Deng, Z. and He, X. Biosynthesis of the β-methylarginine residue of peptidyl nucleoside arginomycin in Streptomyces arginensis NRRL 15941. Appl. Environ. Microbiol. 80 (2014) 5021–5027. [DOI] [PMID: 24907335] |
|
| [EC 2.6.1.125 created 2024] |
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|
| EC |
2.6.1.126 |
| Accepted name: |
L-aspartate:5-guanidino-3-methyl-2-oxopentanoate transaminase |
| Reaction: |
L-aspartate + (3R)-5-guanidino-3-methyl-2-oxopentanoate = oxaloacetate + (3R)-3-methyl-L-arginine |
| Other name(s): |
argM (gene name); mrsB (gene name) |
| Systematic name: |
L-aspartate:5-guanidino-3-methyl-2-oxopentanoate aminotransferase |
| Comments: |
Requires pyridoxal 5′-phosphate. The enzyme, characterized from several bacterial species, participates in the biosynthesis of the rare amino acid (3R)-3-methyl-L-arginine. The enzyme from Streptomyces arginensis also catalyses the activity of EC 2.6.1.125, L-arginine:2-oxoglutarate transaminase. |
| 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] |
| 2. |
Feng, J., Wu, J., Gao, J., Xia, Z., Deng, Z. and He, X. Biosynthesis of the β-methylarginine residue of peptidyl nucleoside arginomycin in Streptomyces arginensis NRRL 15941. Appl. Environ. Microbiol. 80 (2014) 5021–5027. [DOI] [PMID: 24907335] |
|
| [EC 2.6.1.126 created 2024] |
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