ExplorEnz: EC 2.3.1.329

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2.3.1.329

Accepted name:

isonitrile lipopeptide synthase

Reaction:

2 (3R)-3-isocyanobutanoyl-[acyl-carrier protein] + L-lysyl-[L-lysyl-carrier protein] + 2 NADPH = (3R)-N-[(2S)-1-hydroxy-6-[(3R)-3-isocyanobutanamido]hexan-2-yl]-3-isocyanobutanamide + [L-lysyl-carrier protein] + 2 [acyl-carrier protein] + 2 NADP⁺

Other name(s):

scoA (gene name); mmaA (gene name)

Systematic name:

(3R)-3-isocyano-fatty acyl-[acyl-carrier protein]:L-lysyl-[L-lysyl-carrier protein] (3R)-3-isocyano-fatty acyltransferase (hydrolysing)

Comments:

The enzyme, found in some actinobacterial species, is a non-ribosomal peptide synthase (NRPS). Adenylation and thiolation domains of the enzyme activate a lysine residue and load it on the enzyme (this activity is described separately as EC 6.2.1.77, L-lysine—[L-lysyl-carrier protein] ligase). A condensation domain catalyses the condensation of two isonitrile-containing moieties to both amino groups of the lysine, a rare activity in non-ribosomal peptide biosynthesis. A reductase domain catalyses a four-electron reduction, releasing the product from the NRPS with a terminal alcohol group.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Chhabra, A., Haque, A.S., Pal, R.K., Goyal, A., Rai, R., Joshi, S., Panjikar, S., Pasha, S., Sankaranarayanan, R. and Gokhale, R.S. Nonprocessive [2 + 2]e- off-loading reductase domains from mycobacterial nonribosomal peptide synthetases. Proc. Natl. Acad. Sci. USA 109 (2012) 5681–5686. [DOI] [PMID: 22451903]
2.	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]

[EC 2.3.1.329 created 2025]