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Cover Feature: An Unusual Fatty Acyl:Adenylate Ligase (FAAL)–Acyl Carrier Protein (ACP) Didomain in Ambruticin Biosynthesis (ChemBioChem 10/2018)
Author(s) -
Hemmerling Franziska,
Lebe Karen E.,
Wunderlich Johannes,
Hahn Frank
Publication year - 2018
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.201800207
Subject(s) - dna ligase , biosynthesis , polyketide , acyl carrier protein , biochemistry , adenylate kinase , chemistry , substrate (aquarium) , natural product , enzyme , stereochemistry , biology , ecology
The cover feature picture shows the adenylate‐forming‐acyl carrier protein (AFD‐ACP) didomain AmbG in action. This enzyme activates the product of the divinylcyclopropane‐forming rearrangement in ambruticin biosynthesis for further assembly‐line processing. Its biosynthetic role is indicated by its representation as a tamer in the ring. Bioinformatic analysis and in vitro experiments assigned the AFD of AmbG as a fatty acyl:adenylate ligase (FAAL) with an unusually broad substrate tolerance, thus suggesting that its natural substrate might indeed be a polyketide. More information can be found in the communication by F. Hahn et al. on page 1006 in Issue 10, 2018 (DOI: 10.1002/cbic.201800084).