In:
Angewandte Chemie, Wiley, Vol. 134, No. 35 ( 2022-08-26)
Abstract:
Nonribosomal peptide synthetases (NRPSs) can incorporate nonproteinogenic amino acids into peptidyl backbones to increase structural diversity. Genome mining of Schlegelella brevitalea led to the identification of a class of linear lipoheptapeptides, glidomides, featuring two unusual residues: threo ‐β‐OH‐L‐His and threo ‐β‐OH‐D‐Asp. The β‐hydroxylation of Asp and His is catalyzed by the nonheme Fe II /α‐ketoglutarate‐dependent β‐hydroxylases GlmD and GlmF, respectively. GlmD independently catalyzes the hydroxylation of L‐Asp to primarily produce threo ‐β‐OH‐L‐Asp on the thiolation domain, and then undergoes epimerization to form threo ‐β‐OH‐D‐Asp in the final products. However, β‐hydroxylation of His requires the concerted action of GlmF and the interface (I) domain, a novel condensation domain family clade. The key sites of I domain for interaction with GlmF were identified, suggesting that the mechanism for hydroxylation of His depends on the collaboration between hydroxylase and NRPS.
Type of Medium:
Online Resource
ISSN:
0044-8249
,
1521-3757
DOI:
10.1002/ange.v134.35
DOI:
10.1002/ange.202203591
Language:
English
Publisher:
Wiley
Publication Date:
2022
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