Understanding promiscuous amidase activity of an esterase from Bacillus subtilis.
Kourist
Robert
R
Institute of Biochemistry, Department of Biotechnology & Enzyme Catalysis, Greifswald University, Felix-Hausdorff-Strasse 4, 17487 Greifswald, Germany.
Bartsch
Sebastian
S
Fransson
Linda
L
Hult
Karl
K
Bornscheuer
Uwe T
UT
D000577:Amides / Q000378:metabolism; D000581:Amidohydrolases / Q000378:metabolism*; D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000201:enzymology*; D020134:Catalytic Domain; D003198:Computer Simulation; D004950:Esterases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D004952:Esters / Q000378:metabolism; D006860:Hydrogen Bonding; D006868:Hydrolysis; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D013379:Substrate Specificity; D013816:Thermodynamics
D000577:Amides; D004952:Esters; D004950:Esterases; D000581:Amidohydrolases; C019665:amidase