Bacillus anthracis ω-amino acid:pyruvate transaminase employs a different mechanism for dual substrate recognition than other amine transaminases

Applied Microbiology and Biotechnology
Fabian Steffen-MunsbergMatthias Höhne

Abstract

Understanding the metabolic potential of organisms or a bacterial community based on their (meta) genome requires the reliable prediction of an enzyme's function from its amino acid sequence. Besides a remarkable development in prediction algorithms, the substrate scope of sequences with low identity to well-characterized enzymes remains often very elusive. From a recently conducted structure function analysis study of PLP-dependent enzymes, we identified a putative transaminase from Bacillus anthracis (Ban-TA) with the crystal structure 3N5M (deposited in the protein data bank in 2011, but not yet published). The active site residues of Ban-TA differ from those in related (class III) transaminases, which thereby have prevented function predictions. By investigating 50 substrate combinations its amine and ω-amino acid:pyruvate transaminase activity was revealed. Even though Ban-TA showed a relatively narrow amine substrate scope within the tested substrates, it accepts 2-propylamine, which is a prerequisite for industrial asymmetric amine synthesis. Structural information implied that the so-called dual substrate recognition of chemically different substrates (i.e. amines and amino acids) differs from that in formerly known enz...Continue Reading

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Citations

Dec 20, 2017·World Journal of Microbiology & Biotechnology·Erica E Ferrandi, Daniela Monti
Apr 18, 2020·Applied Microbiology and Biotechnology·Stephen A KellyBrendan F Gilmore
Jan 29, 2020·ACS Chemical Biology·Moritz VossUwe T Bornscheuer

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