Characterization of xenobiotic reductase A (XenA): study of active site residues, substrate spectrum and stability.
Xenobiotic reductase A (XenA) has broad catalytic activity and reduces various α,β-unsaturated and nitro compounds with moderate to excellent stereoselectivity. Single mutants C25G and C25V are able to reduce nitrobenzene, a non-active substrate for the wild type, to produce aniline. Total turnover is dominated by chemical rather than thermal instability.
School of Chemical and Biomolecular Engineering, Parker H. Petit Institute of Bioengineering and Biosciences, Georgia Institute of Technology, 315 Ferst Drive, Atlanta, GA, USA.
Yanto
Y
Yanto
Hua-Hsiang
HH
Yu
Mélanie
M
Hall
Andreas S
AS
Bommarius
D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D055162:Biocatalysis; D020134:Catalytic Domain; D004795:Enzyme Stability; D005420:Flavoproteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D015394:Molecular Structure; D009154:Mutation; D009574:Nitro Compounds / Q000737:chemistry; D010088:Oxidoreductases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D013237:Stereoisomerism
D001426:Bacterial Proteins; D005420:Flavoproteins; D009574:Nitro Compounds; C122134:XenA protein, Pseudomonas putida; D010088:Oxidoreductases