Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
6531191 | Journal of Molecular Catalysis B: Enzymatic | 2014 | 7 Pages |
Abstract
- A meso-2, 3-butanediol dehydrogenase from Bacillus subtilis was expressed in E. coli and characterized.
- Amino acid sequence alignment revealed a mutation from Asp to Gly at site 194.
- The substitution maintained substrate-binding ability of the enzyme but severely weaken its catalytic activity.
- Structural modifications of the enzyme might be the major reason causing the lack of enzyme activity.
Keywords
MALDI-TOFBDHTRISAcetoinIPTGDTTITCBacillus subtilisPMSF2,3-Butanediol dehydrogenase2-amino-2-hydroxymethyl-propane-1,3-diol2,3-ButanediolNAD+nicotinamide adenine dinucleotide (reduced form)EDTATrypsin digestionDiacetylcircular dichroismphenylmethylsulfonyl fluoridematrix-assisted laser desorption/ionization time of flightNADHIsothermal titration calorimetry
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Catalysis
Authors
Wenbo Hao, Fangling Ji, Jingyun Wang, Yue Zhang, Tianqi Wang, Yongming Bao,