Identification of aspirinase with one of the carboxylesterases requiring a thiol group

White, Kenneth; Hope, D. B.

doi:10.1042/bj1970771

Cited by 15 publications

(4 citation statements)

References 13 publications

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“…The N-terminal amino acid sequence of GHA deacetylase (Table 3) is similar to those reported for guinea-pig and rat carboxylesterases [36]. Several kinds of deacetylase activity in guinea-pig liver microsomes have been reported [29,36,[42][43][44][45][46][47][48][49][50]. Among these enzymes, the following are thought to resemble GHA deacetylase : the deacetylase of N-hydroxy-N-2-fluorenylacetamide with a molecular mass of 200 kDa [29], and GPH1, a trimeric protein of pI 5.3 composed of subunits with a molecular mass of 57 kDa [36].…”

Section: Discussionsupporting

confidence: 54%

Purification and characterization of guinea-pig liver microsomal deacetylase involved in the deacetylation of the O-glucoside of N-hydroxyacetanilide

Suzuki-Kurasaki

Yoshioka

Uematsu

1997

Biochemical Journal

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A microsomal deacetylase that catalyses the deacetylation of the O-glucoside of N-hydroxyacetanilide (GHA) was purified from guinea-pig liver. The activity was located exclusively in the microsomes and not detected in the cytosol. The purified GHA deacetylase was a trimeric protein with a molecular mass of 160±10 (S.D.) kDa composed of subunits of 53±2 kDa; its pI was 4.7. The N-terminal amino acid sequence of GHA deacetylase was similar to those reported for guinea-pig and rat liver microsomal carboxylesterases. The GHA deacetylase showed a comparable hydrolytic activity towards p-nitrophenyl acetate (PNPA), although the activities towards N-hydroxyacetanilide, acetanilide and some endogenous acylated compounds were very low or not detectable. The deacetylase activity towards GHA was inhibited by organophosphates but not by p-chloromercuribenzoate, suggesting that GHA deacetylase can be classified as a B-esterase. The enzyme exhibited a positive homotropic co-operativity towards GHA. The values of the Hill coefficient, the half-saturating concentration ([S]0.5) for GHA, and Vmax were 1.59±0.03, 5.51±0.07 mM and 32.5±1.4 μmol/min per mg respectively, at the optimum pH of 8.5. The bell-shaped pH dependence of the Vmax/[S]0.5 profile indicated pKa values attributed to histidine and lysine residues. The study of stoichiometric inhibition by di-isopropyl fluorophosphate and kinetic analysis with the Monod–Wyman–Changeux model suggests that GHA deacetylase has six substrate binding sites and three catalytically essential serine residues per enzyme molecule.

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Section: Discussionsupporting

confidence: 54%

Purification and characterization of guinea-pig liver microsomal deacetylase involved in the deacetylation of the O-glucoside of N-hydroxyacetanilide

Suzuki-Kurasaki

Yoshioka

Uematsu

1997

Biochemical Journal

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“…As for the separation assay, cellular LA was determined by GC-FPD (flame photometric detection) and GC-MS (mass spectrometry) after hydrolytic cleavage of the protein-bound LA by concentrated acid or base at high temperature [25][26][27][28]. Since the GC methods included the strong acid and base hydrolysis of the proteins containing LA, the resulting amounts were the sum of the protein-bound LA and free LA (non-protein LA) in the sample.…”

Section: Introductionmentioning

confidence: 99%

Selective and sensitive determination of lipoyllysine (protein-bound α-lipoic acid) in biological specimens by high-performance liquid chromatography with fluorescence detection

Satoh

Shindoh

Min

et al. 2008

Analytica Chimica Acta

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“…Esterases catalyze the hydrolysis of aliphatic and aromatic esters and have been widely studied because of their metabolic functions (29), their utility in flavor development (11), and their role in the breakdown of insecticides (10).…”

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Purification and Properties of an Esterase from the Yeast Saccharomyces cerevisiae and Identification of the Encoding Gene

Degrassi¹,

Uotila

Klima

et al. 1999

Appl Environ Microbiol

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We purified an intracellular esterase that can function as anS-formylglutathione hydrolase from the yeastSaccharomyces cerevisiae. Its molecular mass was 40 kDa, as determined by gel filtration and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The isoelectric point was 5.0 by isoelectric focusing. The enzyme activity was optimal at 50°C and pH 7.0. The corresponding gene, YJLO68C, was identified by its N-terminal amino acid sequence and is not essential for cell viability. Null mutants have reduced esterase activities and grow slowly in the presence of formaldehyde. This enzyme may be involved in the detoxification of formaldehyde, which can be metabolized toS-formylglutathione by S. cerevisiae.

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Identification of aspirinase with one of the carboxylesterases requiring a thiol group

Cited by 15 publications

References 13 publications

Purification and characterization of guinea-pig liver microsomal deacetylase involved in the deacetylation of the O-glucoside of N-hydroxyacetanilide

Purification and characterization of guinea-pig liver microsomal deacetylase involved in the deacetylation of the O-glucoside of N-hydroxyacetanilide

Selective and sensitive determination of lipoyllysine (protein-bound α-lipoic acid) in biological specimens by high-performance liquid chromatography with fluorescence detection

Purification and Properties of an Esterase from the Yeast Saccharomyces cerevisiae and Identification of the Encoding Gene

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