The Enzyme Database

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Accepted name: (R)-3-[(carboxymethyl)amino]fatty acid dioxygenase/decarboxylase
Reaction: a (3R)-3-[(carboxylmethyl)amino]fatty acid + 2 2-oxoglutarate + 2 O2 = a (3R)-3-isocyanyl-fatty acid + 2 succinate + 3 CO2 + 2 H2O (overall reaction)
(1a) a (3R)-3-[(carboxylmethyl)amino]fatty acid + 2-oxoglutarate + O2 = a (3R)-3-{[carboxy(hydroxy)methyl]amino}fatty acid + succinate + CO2
(1b) a (3R)-3-{[carboxy(hydroxy)methyl]amino}fatty acid + 2-oxoglutarate + O2 = a (3R)-3-isocyanyl-fatty acid + succinate + 2 CO2 + 2 H2O
Other name(s): scoE (gene name); mmaE (gene name); Rv0097 (locus name)
Systematic name: (3R)-3-[(carboxylmethyl)amino]fatty acid,2-oxoglutarate:oxygen oxidoreductase (isonitrile-forming)
Comments: Requires Fe(II). The enzyme, found in actinobacterial species, participates in the biosynthesis of isonitrile-containing lipopeptides. The reaction comprises two catalytic cycles, each consuming an oxygen molecule and a 2-oxoglutarate molecule. In the first cycle the substrate is hydroxylated, while in the second cycle the enzyme catalyses a decarboxylation/oxidation reaction that produces an isonitrile group.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Harris, N.C., Sato, M., Herman, N.A., Twigg, F., Cai, W., Liu, J., Zhu, X., Downey, J., Khalaf, R., Martin, J., Koshino, H. and Zhang, W. Biosynthesis of isonitrile lipopeptides by conserved nonribosomal peptide synthetase gene clusters in Actinobacteria. Proc. Natl. Acad. Sci. USA 114 (2017) 7025–7030. [DOI] [PMID: 28634299]
2.  Harris, N.C., Born, D.A., Cai, W., Huang, Y., Martin, J., Khalaf, R., Drennan, C.L. and Zhang, W. Isonitrile formation by a non-heme iron(II)-dependent oxidase/decarboxylase. Angew. Chem. Int. Ed. Engl. 57 (2018) 9707–9710. [DOI] [PMID: 29906336]
3.  Jonnalagadda, R., Del Rio Flores, A., Cai, W., Mehmood, R., Narayanamoorthy, M., Ren, C., Zaragoza, J.PT., Kulik, H.J., Zhang, W. and Drennan, C.L. Biochemical and crystallographic investigations into isonitrile formation by a nonheme iron-dependent oxidase/decarboxylase. J. Biol. Chem. 296:100231 (2021). [DOI] [PMID: 33361191]
[EC created 2022]

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