The Enzyme Database

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EC 2.1.1.316     
Accepted name: mitomycin 6-O-methyltransferase
Reaction: (1) S-adenosyl-L-methionine + 6-demethylmitomycin A = S-adenosyl-L-homocysteine + mitomycin A
(2) S-adenosyl-L-methionine + 6-demethylmitomycin B = S-adenosyl-L-homocysteine + mitomycin B
Glossary: mitomycin A = [(1aS,8S,8aR,8bS)-5-methyl-6,8a-dimethoxy-4,7-dioxo-1,1a,2,4,7,8,8a,8b-octahydroazirino[2′,3′:3,4]pyrrolo[1,2-a]indol-8-yl]methyl carbamate
mitomycin B = [(1aS,8S,8aR,8bS)-8a-hydroxy-5-methyl-6-methoxy-4,7-dioxo-1,1a,2,4,7,8,8a,8b-octahydroazirino[2′,3′:3,4]pyrrolo[1,2-a]indol-8-yl]methyl carbamate
Other name(s): MmcR; mitomycin 7-O-methyltransferase (incorrect); S-adenosyl-L-methionine:7-demethylmitomycin-A 7-O-methyltransferase (incorrect)
Systematic name: S-adenosyl-L-methionine:6-demethylmitomycin-A 6-O-methyltransferase
Comments: The enzyme, characterized from the bacterium Streptomyces lavendulae, is involved in the biosynthesis of the quinone-containing antibiotics mitomycin A and mitomycin B.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Gruschow, S., Chang, L.C., Mao, Y. and Sherman, D.H. Hydroxyquinone O-methylation in mitomycin biosynthesis. J. Am. Chem. Soc. 129 (2007) 6470–6476. [DOI] [PMID: 17461583]
2.  Singh, S., Chang, A., Goff, R.D., Bingman, C.A., Gruschow, S., Sherman, D.H., Phillips, G.N., Jr. and Thorson, J.S. Structural characterization of the mitomycin 7-O-methyltransferase. Proteins 79 (2011) 2181–2188. [DOI] [PMID: 21538548]
[EC 2.1.1.316 created 2015]
 
 
EC 4.2.1.144     
Accepted name: 3-amino-5-hydroxybenzoate synthase
Reaction: 5-amino-5-deoxy-3-dehydroshikimate = 3-amino-5-hydroxybenzoate + H2O
Other name(s): AHBA synthase; rifK (gene name)
Systematic name: 5-amino-5-deoxy-3-dehydroshikimate hydro-lyase (3-amino-5-hydroxybenzoate-forming)
Comments: A pyridoxal 5′-phosphate enzyme. The enzyme from the bacterium Amycolatopsis mediterranei participates in the pathway for rifamycin B biosynthesis. The enzyme also functions as a transaminase earlier in the pathway, producing UDP-α-D-kanosamine [3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Kim, C.G., Yu, T.W., Fryhle, C.B., Handa, S. and Floss, H.G. 3-Amino-5-hydroxybenzoic acid synthase, the terminal enzyme in the formation of the precursor of mC7N units in rifamycin and related antibiotics. J. Biol. Chem. 273 (1998) 6030–6040. [DOI] [PMID: 9497318]
2.  Eads, J.C., Beeby, M., Scapin, G., Yu, T.W. and Floss, H.G. Crystal structure of 3-amino-5-hydroxybenzoic acid (AHBA) synthase. Biochemistry 38 (1999) 9840–9849. [DOI] [PMID: 10433690]
3.  Floss, H.G., Yu, T.W. and Arakawa, K. The biosynthesis of 3-amino-5-hydroxybenzoic acid (AHBA), the precursor of mC7N units in ansamycin and mitomycin antibiotics: a review. J. Antibiot. (Tokyo) 64 (2011) 35–44. [DOI] [PMID: 21081954]
[EC 4.2.1.144 created 2013]
 
 


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