Site-directed mutagenesis of residues in coenzyme-binding domain and active site of mouse lung carbonyl reductase.
Nakanishi
M
M
Department of Applied Chemistry, Faculty of Engineering, Gifu University, Japan.
Kaibe
H
H
Matsuura
K
K
Kakumoto
M
M
Tanaka
N
N
Nonaka
T
T
Mitsui
Y
Y
Hara
A
A
D000429:Alcohol Oxidoreductases / Q000737:chemistry* / Q000378:metabolism*; D000449:Aldehyde Reductase; D000074408:Aldo-Keto Reductases; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D003001:Cloning, Molecular; D016384:Consensus Sequence; D018360:Crystallography, X-Ray; D004926:Escherichia coli; D006801:Humans; D007700:Kinetics; D008168:Lung / Q000201:enzymology*; D051379:Mice; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D009249:NADP / Q000378:metabolism / Q000494:pharmacology; D017354:Point Mutation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity
D011994:Recombinant Proteins; D009249:NADP; D000429:Alcohol Oxidoreductases; D000074408:Aldo-Keto Reductases; D000449:Aldehyde Reductase; C000614209:AKR7A5 protein, mouse