Purification and characterization of an esterase from Micrococcus sp. YGJ1 hydrolyzing phthalate esters.
An esterase hydrolyzing phthalate esters has been purified from Micrococcus sp. YGJ1. The enzyme, a monomeric protein (Mr = 56 kDa) with a pI of 4.0, hydrolyzes various aliphatic and aromatic carboxylesters. The medium chain (C3-C4) esters are the most preferred substrates. The enzyme is inhibited by HgCl2 and p-chloromercuribenzoate but not by phenylmethylsulfonyl fluoride.
Akita
K
K
Department of Biomolecular Science, Faculty of Engineering, Gifu University, Japan.
Naitou
C
C
Maruyama
K
K
D003993:Dibutyl Phthalate / Q000378:metabolism; D004791:Enzyme Inhibitors / Q000494:pharmacology; D004950:Esterases / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D006868:Hydrolysis; D007526:Isoelectric Point; D007700:Kinetics; D008627:Mercuric Chloride / Q000494:pharmacology; D008837:Micrococcus / Q000201:enzymology*; D008970:Molecular Weight; D009596:Nitrophenols / Q000378:metabolism; D010795:Phthalic Acids / Q000378:metabolism; D013379:Substrate Specificity; D020245:p-Chloromercuribenzoic Acid / Q000494:pharmacology
D004791:Enzyme Inhibitors; D009596:Nitrophenols; D010795:Phthalic Acids; D003993:Dibutyl Phthalate; D008627:Mercuric Chloride; D020245:p-Chloromercuribenzoic Acid; C008642:4-nitrophenyl acetate; D004950:Esterases