科研之友
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摘要
omega-Aminotransferase (omega-AT) is an important class of enzymes for the synthesis of chiral amines or beta-amino acids. Family profile analysis was applied to screen putative omega-ATs from Mesorhizobium loti MAFF303099, a nitrogen fixation bacterium that has a larger number of ATs than other microorganisms. By family profile analysis, we selected 10 putative omega-ATs according to E-value. The functions of the putative omega-ATs were investigated by examining activities towards amines and/or beta-amino acids. 10 putative proteins were found to have omega-AT activity with narrow or broad substrate specificity. Structure analysis using crystal structure of mll7127 and homology models of mll1632 and mll3663 indicated that the structures of active sites of the enzymes were very similar and highly conserved, but their substrate specificities appreared to be determined by residues positioned at the entrance region of the active site binding pockets.
- 出版日期2012-7
