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Cover Feature: Crystal Structure of PigA: A Prolyl Thioester‐Oxidizing Enzyme in Prodigiosin Biosynthesis (ChemBioChem 2/2019)
Author(s) -
Lee ChengChung,
Ko TzuPing,
Chen ChunTing,
Chan YuehTe,
Lo ShinYi,
Chang JenYu,
Chen YaWen,
Chung TingFang,
Hsieh HsinJu,
Hsiao ChwanDeng,
Wang Andrew H.J.
Publication year - 2019
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.201800805
Subject(s) - prodigiosin , biosynthesis , pyrrole , chemistry , serratia marcescens , stereochemistry , enzyme , biochemistry , organic chemistry , escherichia coli , gene
The cover feature picture shows the biosynthetic pathway of the three‐pyrrole red pigment prodigiosin in Serratia marcescens , the historical culprit of bleeding bread. The tetrameric enzyme PigA oxidizes carrier‐bound proline and turns out the first pyrrole unit of MBC, which then combines with MAP to form the final product. More information can be found in the full paper by C.‐D. Hsiao, A. H.‐J. Wang et al. on page 193 in Issue 2, 2019 (DOI: 10.1002/cbic.201800409).