KEGG   ENZYME: 6.2.1.62Help
Entry
EC 6.2.1.62                 Enzyme                                 

Name
3,4-dihydroxybenzoate---[aryl-carrier protein] ligase;
asbC (gene name)
Class
Ligases;
Forming carbon-sulfur bonds;
Acid-thiol ligases
BRITE hierarchy
Sysname
3,4-dihydroxybenzoate:[aryl-carrier protein] ligase (AMP-forming)
Reaction(IUBMB)
ATP + 3,4-dihydroxybenzoate + holo-[aryl-carrier protein] = AMP + diphosphate + 3,4-dihydroxybenzoyl-[aryl-carrier protein] (overall reaction);
(1a) ATP + 3,4-dihydroxybenzoate = diphosphate + (3,4-dihydroxybenzoyl)adenylate [RN:R12576];
(1b) (3,4-dihydroxybenzoyl)adenylate + holo-[aryl-carrier protein] = AMP + 3,4-dihydroxybenzoyl-[aryl-carrier protein]
Reaction(KEGG)
R12576;
(other) R12575 R12577
Show
Substrate
ATP [CPD:C00002];
3,4-dihydroxybenzoate [CPD:C00230];
holo-[aryl-carrier protein] [CPD:C20665];
(3,4-dihydroxybenzoyl)adenylate [CPD:C20884]
Product
AMP [CPD:C00020];
diphosphate [CPD:C00013];
3,4-dihydroxybenzoyl-[aryl-carrier protein] [CPD:C20883];
(3,4-dihydroxybenzoyl)adenylate [CPD:C20884]
Comment
The adenylation domain of the enzyme catalyses the activation of 3,4-dihydroxybenzoate to (3,4-dihydroxybenzoyl)adenylate, followed by the transfer of the activated compound to the free thiol of a phosphopantetheine arm of an aryl-carrier protein domain. The aryl-carrier protein domain may be part of the same protein, or of a different protein. This activity is often found as part of a larger non-ribosomal peptide synthase.
History
EC 6.2.1.62 created 2020
Reference
1  [PMID:17346033]
  Authors
Pfleger BF, Lee JY, Somu RV, Aldrich CC, Hanna PC, Sherman DH
  Title
Characterization and analysis of early enzymes for petrobactin biosynthesis in Bacillus anthracis.
  Journal
Biochemistry 46:4147-57 (2007)
DOI:10.1021/bi6023995
  Sequence
[ban:BA_1983]
Other DBs
ExplorEnz - The Enzyme Database: 6.2.1.62
IUBMB Enzyme Nomenclature: 6.2.1.62
ExPASy - ENZYME nomenclature database: 6.2.1.62
BRENDA, the Enzyme Database: 6.2.1.62

DBGET integrated database retrieval system