ExplorEnz: EC 2.6.1.114

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2.6.1.114

Accepted name:

8-demethyl-8-aminoriboflavin-5′-phosphate synthase

Reaction:

L-glutamate + FMN + O₂ + H₂O + 3 acceptor = 2-oxoglutarate + 8-amino-8-demethylriboflavin 5′-phosphate + CO₂ + 3 reduced acceptor (overall reaction)
(1a) FMN + O₂ = 8-demethyl-8-formylriboflavin 5′-phosphate + H₂O
(1b) 8-demethyl-8-formylriboflavin 5′-phosphate + H₂O + acceptor = 8-carboxy-8-demethylriboflavin 5′-phosphate + reduced acceptor
(1c) L-glutamate + 8-carboxy-8-demethylriboflavin 5′-phosphate + H₂O + 2 acceptor = 2-oxoglutarate + 8-amino-8-demethylriboflavin 5′-phosphate + CO₂ + 2 reduced acceptor

For diagram of roseoflavin biosynthesis, click here

Glossary:

roseoflavin = 8-demethyl-8-(dimethylamino)riboflavin

Other name(s):

rosB (gene name)

Systematic name:

L-glutamate:FMN aminotransferase (oxidizing, decarboxylating)

Comments:

The enzyme, characterized from the bacterium Streptomyces davawensis, has the activities of an oxidoreductase, a decarboxylase, and an aminotransferase. Its combined actions result in the replacement of a methyl substituent of one of the aromatic rings of FMN by an amino group, a step in the biosynthetic pathway of roseoflavin. The reaction requires thiamine for completion.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Schwarz, J., Konjik, V., Jankowitsch, F., Sandhoff, R. and Mack, M. Identification of the key enzyme of roseoflavin biosynthesis. Angew. Chem. Int. Ed. Engl. 55 (2016) 6103–6106. [DOI] [PMID: 27062037]
2.	Jhulki, I., Chanani, P.K., Abdelwahed, S.H. and Begley, T.P. A remarkable oxidative cascade that replaces the riboflavin C₈ methyl with an amino group during roseoflavin biosynthesis. J. Am. Chem. Soc. 138 (2016) 8324–8327. [DOI] [PMID: 27331868]
3.	Konjik, V., Brunle, S., Demmer, U., Vanselow, A., Sandhoff, R., Ermler, U. and Mack, M. The crystal structure of RosB: insights into the reaction mechanism of the first member of a family of flavodoxin-like enzymes. Angew. Chem. Int. Ed. Engl. 56 (2017) 1146–1151. [DOI] [PMID: 27981706]

[EC 2.6.1.114 created 2018]