|
type |
Journal Article |
authors |
Muliandi A, Katsuyama Y, Sone K, Izumikawa M2, Moriya T, Hashimoto J, Kozone I, Takagi M, Shin-ya K, Ohnishi Y. |
title |
Biosynthesis of the 4-methyloxazoline-containing nonribosomal peptides, JBIR-34 and -35, in Streptomyces sp. Sp080513GE-23 |
journal |
Chem Biol |
Activity |
2.1.2.7 |
Family |
2.1.2.7.b |
PLP Fold Type |
1 |
sel |
selected |
ui |
25041948 |
year |
(2014) |
volume |
21 |
number |
8 |
pages |
923-34 |
| |
keywords |
doi 10.1016/j.chembiol.2014.06.004 |
abstract |
JBIR-34 and -35 produced by Streptomyces sp. Sp080513GE-23 are nonribosomal peptides that possess an unusual 4-methyloxazoline moiety. Through draft genome sequencing, cosmid cloning, and gene disruption, the JBIR-34 and -35 biosynthesis gene cluster (fmo cluster) was identified; it encodes 20 proteins including five nonribosomal peptide synthetases (NRPSs). Disruption of one of these NRPS genes (fmoA3) resulted in no JBIR-34 and -35 production and accumulation of 6-chloro-4-hydroxyindole-3-carboxylic acid. Stable isotope-feeding experiments indicated that the methyl group of the methyloxazoline ring is derived from alanine rather than methionine. A recombinant FmoH protein, a glycine/serine hydroxymethyltransferase homolog, catalyzed conversion of α-methyl-l-serine into d-alanine (the reverse reaction of α-methyl-l-serine synthesis catalyzed by FmoH in vivo). Taken together, we concluded that α-methyl-l-serine synthesized from d-alanine is incorporated into JBIR-34 and -35 to form the 4-methyloxazoline moiety. We also propose the biosynthesis pathway of JBIR-34 and -35. |
last changed |
2018/11/21 17:36 |
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