Topic
Esterase
About: Esterase is a research topic. Over the lifetime, 7622 publications have been published within this topic receiving 168270 citations.
Papers published on a yearly basis
Papers
More filters
TL;DR: A new species of gram-negative, rod-shaped, motile bacteria that were nonhemolytic on blood agar and were isolated from clinical sources are proposed, including P. monteilii, which was capable of respiratory but not fermentative metabolism.
Abstract: We propose the name Pseudomonas monteilii for a new species of gram-negative, rod-shaped, motile bacteria that were nonhemolytic on blood agar and were isolated from clinical sources. The 10 strains of P. monteilii were incapable of liquefing gelatin. They grew at 10°C but not at 41°C, produced fluorescent pigments, catalase, and cytochrome oxidase, and possessed the arginine dihydrolase system. They were capable of respiratory but not fermentative metabolism. They did not hydrolyze esculin or starch and were able to use benzylamine, α-aminobutyrate, d-ribose, l-arabinose, butyrate, valerate, isovalerate, isobutyrate, inositol, phenylacetate, d-alanine, and amylamine. They possessed l-phenylalanine arylamidase, l-lysine arylamidase, l-alanine arylamidase, γ-glutamyl-transferase, glycyl -phenylalanine arylamidase, l-tryptophan arylamidase, glycyl-l-alanine arylamidase, esterase C4, esterase C6, esterase C8, esterase C9, esterase C10, and esterase C18. DNA relatedness studies revealed that P. monteilii strains formed a homogeneous DNA hybridization group. A total of 57 strains representing previously described or partially characterized taxa belonging to the genus Pseudomonas were 6 to 54% related to P. monteilii. The highest hybridization values were obtained with strains belonging to or related to Pseudomonas putida biovar A. The average G+C content of the DNA was 60.5 ± 0.5 mol% for four of the P. monteilii strains studied. The type strain of P. monteilii is CFML 90-60 (= CIP 104883); it was isolated from bronchial aspirate and has a G+C content of 60 mol%. The clinical significance of these organisms is not known.
93 citations
TL;DR: The study confirms the ability of physiologically important esterases to catalyze the hydrolysis of biomaterial methacrylates.
Abstract: This study addressed whether methacrylate monomers and polymers used in dentistry might degrade from enzymolysis by acetylcholinesterase (ACHE), cholesterol esterase (CHE), porcine liver esterase (PRLE), and a pancreatic lipase (PNL). Short (hour) and long-term (day) exposures were performed. Product ratios were used to determine surface hydrolysis of the polymeric materials. Enzyme kinetics were studied for the monomers when challenged by ACHE, CHE, and PRLE. In the case of PRLE, the Vmax for the dimethacrylate substrates varied slightly, but amounted to as much as 10% of that of p-nitrophenylacetate. The Km for triethylene glycol dimethacrylate (TEGDMA) was 197 μM for ACHE and 1107 μM for CHE. The Vmax was 2.7 nmol/min for ACHE and 3.5 nmol/min for CHE. TEGDMA was converted by CHE at 2% the rate of cholesteryl oleate. Long-term incubations of monomers with CHE and ACHE produced degrees of hydrolysis that evidenced structure dependency in the ability of the enzymes to effect hydrolysis. Particularly resistant were aromativ derivatives and those with branching in methacrylate linkages. Overall, the study confirms the ability of physiologically important esterases to catalyze the hydrolysis of biomaterial methacrylates. © 2001 John Wiley & Sons, Inc. J Biomed Mater Res 57: 522–531, 2001
93 citations
TL;DR: Synergistic effects were observed between the esterase and other xylan-degrading enzymes in hydrolyzing the ferulic and, to a lesser extent, the ϱ-coumaric acid esters from both wheat straw xylan and the grass cell walls.
93 citations
TL;DR: The kinetic properties of acid cholesteryl esterase in preparations of rabbit aortic cells, with the aim of establishing conditions suitable for the quantitative assay of the enzyme in freshly prepared homogenates and subcellular fractions, support the hypothesis that lipid overloading of lysosomes in atheromatous arterial cells occurs as a consequence of a relative deficiency of acid Cholesteryl Esterase.
93 citations
TL;DR: Differences in protease susceptibility can be related to the conformational state of the substrate, and the possible implication of structural changes in the mechanism of preferential proteolysis in vivo is discussed.
93 citations