Premium
Functional and structural characterization of IdnL7, an adenylation enzyme involved in incednine biosynthesis
Author(s) -
Cieślak Jolanta,
Miyanaga Akimasa,
Takaishi Makoto,
Kudo Fumitaka,
Eguchi Tadashi
Publication year - 2019
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x19002863
Subject(s) - adenylylation , biosynthesis , polyketide , enzyme , biochemistry , natural product , amino acid , stereochemistry , chemistry , biology
Adenylation enzymes play an important role in the selective incorporation of the cognate carboxylate substrates in natural product biosynthesis. Here, the biochemical and structural characterization of the adenylation enzyme IdnL7, which is involved in the biosynthesis of the macrolactam polyketide antibiotic incednine, is reported. Biochemical analysis showed that IdnL7 selects and activates several small amino acids. The structure of IdnL7 in complex with an l ‐alanyl‐adenylate intermediate mimic, 5′‐ O ‐[ N ‐( l ‐alanyl)sulfamoyl]adenosine, was determined at 2.1 Å resolution. The structure of IdnL7 explains the broad substrate specificity of IdnL7 towards small l ‐amino acids.