Journal
CHEMBIOCHEM
Volume 13, Issue 12, Pages 1798-1804Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.201200187
Keywords
atromentin; biosynthesis; natural products; nonribosomal peptide synthetase; Suillus
Funding
- Deutsche Forschungsgemeinschaft (DFG) [HO 2515/4-1]
- National Institutes of Health (National Center for Research Resources) [2P41RR001081]
- National Institute of General Medical Sciences [9P41M103311]
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The gene greA was cloned from the genome of the basidiomycete Suillus grevillei. It encodes a monomodular natural product biosynthesis protein composed of three domains for adenylation, thiolation, and thioesterase and, hence, is reminiscent of a nonribosomal peptide synthetase (NRPS). GreA was biochemically characterized in vitro. It was identified as atromentin synthetase and therefore represents one of only a limited number of biochemically characterized NRPS-like enzymes which accept an aromatic a-keto acid. Specificity-conferring amino acid residuescollectively referred to as the nonribosomal codewere predicted for the primary sequence of the GreA adenylation domain and were an unprecedented combination for aromatic a-keto acids. Plausible support for this new code came from in silico simulation of the adenylation domain structure. According to the model, the predicted residues line the active site and, therefore, very likely contribute to substrate specificity.
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