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Back Cover: Minimization of the Thiolactomycin Biosynthetic Pathway Reveals that the Cytochrome P450 Enzyme TlmF Is Required for Five‐Membered Thiolactone Ring Formation (ChemBioChem 12/2017)
Author(s) -
Tang Xiaoyu,
Li Jie,
Moore Bradley S.
Publication year - 2017
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201700270
Subject(s) - thiolactone , stereochemistry , biosynthesis , cytochrome p450 , enzyme , chemistry , natural product , biochemistry
The back cover picture shows the minimization of the thiolactomycin biosynthetic gene cluster from the marine bacterium Salinispora pacifica CNS‐863 as well as the critical role of cytochrome P450 in the biosynthesis of this structurally unique antibiotics family. The CYP450 and three other enzymes (TlmG, TlmH, and TlmI) together are sufficient for the construction of the γ ‐thiolactone skeleton; the δ ‐thiolactone is formed as a shunt product in the absence of this CYP450. Picture: Jie Li and Zhong‐Rui Li. More information can be found in the communication by B. S. Moore et al. on page 1072 in Issue 12, 2017 (DOI: 10.1002/cbic.201700090).