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.
Yanto
Yanto
Y
School of Chemical and Biomolecular Engineering, Parker H. Petit Institute of Bioengineering and Biosciences, Georgia Institute of Technology, 315 Ferst Drive, Atlanta, GA, USA.
Yu
Hua-Hsiang
HH
Hall
Mélanie
M
Bommarius
Andreas S
AS
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