Characterization of the epoxide hydrolase from an epichlorohydrin-degrading Pseudomonas sp.
An epoxide hydrolase was purified to homogeneity from the epichlorohydrin-utilizing bacterium Pseudomonas sp. strain AD1. The enzyme was found to be a monomeric protein with a molecular mass of 35 kDa. With epichlorohydrin as the substrate, the enzyme followed Michaelis-Menten kinetics with a Km value of 0.3 mM and a Vmax of 34 mumol.min-1.mg protein-1. The epoxide hydrolase catalyzed the hydrolysis of several epoxides, including epichlorohydrin, epibromohydrin, epoxyoctane and styrene epoxide. With all chiral compounds tested, both stereoisomers were converted. Amino acid sequencing of cyanogen bromide-generated peptides did not yield sequences with similarities to other known proteins.
Jacobs
M H
MH
Department of Biochemistry, University of Groningen, The Netherlands.
Van den Wijngaard
A J
AJ
Pentenga
M
M
Janssen
D B
DB
D000595:Amino Acid Sequence; D002845:Chromatography; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D017886:Durapatite; D004591:Electrophoresis, Polyacrylamide Gel; D004811:Epichlorohydrin / Q000378:metabolism*; D004851:Epoxide Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D006882:Hydroxyapatites; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010446:Peptide Fragments / Q000302:isolation & purification; D011549:Pseudomonas / Q000201:enzymology*; D013379:Substrate Specificity; D013816:Thermodynamics
D006882:Hydroxyapatites; D010446:Peptide Fragments; D004811:Epichlorohydrin; D017886:Durapatite; D004851:Epoxide Hydrolases