|
type |
Journal Article |
authors |
Takaishi M, Kudo F, Eguchi T. |
title |
Identification of the incednine biosynthetic gene cluster: characterization of novel β-glutamate-β-decarboxylase IdnL3. |
journal |
J Antibiot (Tokyo). |
Activity |
idnl3 |
Family |
idnl3 |
sel |
selected |
ui |
23921821 |
year |
(2013) |
volume |
66 |
number |
12 |
pages |
691-9 |
| |
abstract |
A biosynthetic gene cluster for the 24-membered macrolactam antibiotic incednine was identified from the producer strain, Streptomyces sp. ML694-90F3. Among the putative incednine biosynthetic enzymes, a novel pyridoxal 5'-phosphate (PLP)-dependent β-glutamate-β-decarboxylase, IdnL3, was functionally characterized in vitro by demonstrating its (S)-3-aminobutyrate-forming activity with β-glutamate in the presence of PLP. Because (S)-3-aminobutyrate is known for the direct precursor of incednine, this enzyme supplies the unique β-amino acid starter unit. The identified gene cluster encodes five characteristic β-amino acid carrying enzymes, consisting of a pathway-specific ATP-dependent ligase, a discrete acyl carrier protein (ACP), β-aminoacyl-ACP β-amino group-protecting ATP-dependent ligase, dipeptidyl-ACP:PKS-loading ACP dipeptidyltransferase and a terminal amino acid peptidase, which are completely conserved in β-amino acid-containing macrolactam biosynthetic gene clusters. Overall, a plausible biosynthetic pathway for incednine was proposed. |
last changed |
2014/03/31 12:45 |
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