KEGG ENZYME: 6.3.2.64

ENZYME: 6.3.2.64

Entry

EC 6.3.2.64                 Enzyme

Name

bisucaberin synthase;
pubC (gene name);
BibC C-terminal domain

Class

Ligases;
Forming carbon-nitrogen bonds;
Acid-D-amino-acid ligases (peptide synthases)

Sysname

N1-hydroxy-N1-succinylcadaverine:N1-hydroxy-N1-succinylcadaverine ligase

Reaction(IUBMB)

2 ATP + 2 N1-hydroxy-N1-succinylcadaverine = 2 AMP + 2 diphosphate + bisucaberin (overall reaction) [RN:R13320];
(1a) ATP + 2 N1-hydroxy-N1-succinylcadaverine = AMP + diphosphate + bisucaberin B [RN:R13318];
(1b) ATP + bisucaberin B = AMP + diphosphate + bisucaberin [RN:R13319]

Reaction(KEGG)

R13318 R13319 R13320

Substrate

ATP [CPD:C00002];
N1-hydroxy-N1-succinylcadaverine [CPD:C22915];
bisucaberin B [CPD:C22916]

Product

AMP [CPD:C00020];
diphosphate [CPD:C00013];
bisucaberin [CPD:C22917];
bisucaberin B [CPD:C22916]

Comment

Requires Mg2+. The enzyme, characterized from the bacterium Aliivibrio salmonicida, catalyses the last step in the biosynthesis of the siderophore bisucaberin. The enzyme catalyses the reaction in two steps - concatenation of two molecules of N1-hydroxy-N1-succinylcadaverine, followed by cyclization.

History

EC 6.3.2.64 created 2024

Reference

1 [PMID:18956041]

Authors

Kadi N, Song L, Challis GL.

Title

Bisucaberin biosynthesis: an adenylating domain of the BibC multi-enzyme catalyzes cyclodimerization of N-hydroxy-N-succinylcadaverine.

Journal

Chem Commun (Camb) 5119-21 (2008)
DOI:10.1039/b813029a

Other DBs

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