Molecular basis of perhydrolase activity in serine hydrolases.
Bernhardt
Peter
P
University of Minnesota, Department of Biochemistry, Molecular Biology and Biophysics, The Biotechnology Institute, and The Center for Microbial and Plant Genomics, 1479 Gortner Avenue, St. Paul, Minnesota 55108, USA, Fax: (+1) 612-625-5780.|School of Biotechnology, Department of Biochemistry, Royal Institute of Technology (KTH), AlbaNova University Center, Roslagstullsbacken 21, 10691 Stockholm, Sweden.
Hult
Karl
K
School of Biotechnology, Department of Biochemistry, Royal Institute of Technology (KTH), AlbaNova University Center, Roslagstullsbacken 21, 10691 Stockholm, Sweden.
Kazlauskas
Romas J
RJ
University of Minnesota, Department of Biochemistry, Molecular Biology and Biophysics, The Biotechnology Institute, and The Center for Microbial and Plant Genomics, 1479 Gortner Avenue, St. Paul, Minnesota 55108, USA, Fax: (+1) 612-625-5780.
D000818:Animals; D004950:Esterases / Q000737:chemistry; D004952:Esters / Q000378:metabolism; D006867:Hydrolases / Q000737:chemistry / Q000378:metabolism*; D006868:Hydrolysis; D007700:Kinetics; D008958:Models, Molecular; D015394:Molecular Structure; D010463:Peracetic Acid / Q000737:chemistry / Q000378:metabolism; D017434:Protein Structure, Tertiary; D011551:Pseudomonas fluorescens / Q000201:enzymology; D051381:Rats; D012694:Serine / Q000378:metabolism*; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D004952:Esters; D012694:Serine; D006867:Hydrolases; D004950:Esterases; D010463:Peracetic Acid