Title : Characterization of the Suillus grevillei quinone synthetase GreA supports a nonribosomal code for aromatic alpha-keto acids - Wackler_2012_Chembiochem_13_1798 |
Author(s) : Wackler B , Lackner G , Chooi YH , Hoffmeister D |
Ref : Chembiochem , 13 :1798 , 2012 |
Abstract :
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 alpha-keto acid. Specificity-conferring amino acid residues--collectively referred to as the nonribosomal code--were predicted for the primary sequence of the GreA adenylation domain and were an unprecedented combination for aromatic alpha-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. |
PubMedSearch : Wackler_2012_Chembiochem_13_1798 |
PubMedID: 22730234 |
Gene_locus related to this paper: suigr-grea |
Gene_locus | suigr-grea |
Wackler B, Lackner G, Chooi YH, Hoffmeister D (2012)
Characterization of the Suillus grevillei quinone synthetase GreA supports a nonribosomal code for aromatic alpha-keto acids
Chembiochem
13 :1798
Wackler B, Lackner G, Chooi YH, Hoffmeister D (2012)
Chembiochem
13 :1798