| EC |
2.7.7.97 |
| Accepted name: |
3-hydroxy-4-methylanthranilate adenylyltransferase |
| Reaction: |
ATP + 3-hydroxy-4-methylanthranilate = diphosphate + 3-hydroxy-4-methylanthranilyl-adenylate |
| Other name(s): |
acmA (gene name); sibE (gene name); actinomycin synthase I; 4-MHA-activating enzyme; ACMS I; actinomycin synthetase I; 4-MHA pentapeptide lactone synthase AcmA |
| Systematic name: |
ATP:3-hydroxy-4-methylanthranilate adenylyltransferase |
| Comments: |
The enzyme, characterized from the bacteria Streptomyces anulatus and Streptosporangium sibiricum, activates 3-hydroxy-4-methylanthranilate, a precursor of actinomycin antibiotics and the antitumor antibiotic sibiromycin, to an adenylate form, so it can be loaded onto a dedicated aryl-carrier protein. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Pfennig, F., Schauwecker, F. and Keller, U. Molecular characterization of the genes of actinomycin synthetase I and of a 4-methyl-3-hydroxyanthranilic acid carrier protein involved in the assembly of the acylpeptide chain of actinomycin in Streptomyces. J. Biol. Chem. 274 (1999) 12508–12516. [DOI] [PMID: 10212227] |
| 2. |
Giessen, T.W., Kraas, F.I. and Marahiel, M.A. A four-enzyme pathway for 3,5-dihydroxy-4-methylanthranilic acid formation and incorporation into the antitumor antibiotic sibiromycin. Biochemistry 50 (2011) 5680–5692. [DOI] [PMID: 21612226] |
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| [EC 2.7.7.97 created 2016] |
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