نتایج جستجو برای: d phenylglycine aminotransferase

تعداد نتایج: 591508  

Journal: :The Journal of biological chemistry 1986
J M Kim S Shimizu H Yamada

N-Carbamoylsarcosine amidohydrolase, a novel enzyme involved in the microbial degradation of creatinine in Pseudomonas putida 77, was purified 27-fold to homogeneity with a 63% overall recovery through simple purification procedures including successive ammonium sulfate fractionation, DEAE-cellulose chromatography, and crystallization. The relative molecular mass of the native enzyme estimated ...

Journal: :Applied and environmental microbiology 1993
H F Hermes T Sonke P J Peters J A van Balken J Kamphuis L Dijkhuizen E M Meijer

An l-aminopeptidase of Pseudomonas putida, used in an industrial process for the hydrolysis of d,l-amino acid amide racemates, was purified to homogeneity. The highly l-enantioselective enzyme resembled thiol reagent-sensitive alkaline serine proteinases and was strongly activated by divalent cations. It possessed a high substrate specificity for dipeptides and alpha-H amino acid amides, e.g., ...

Journal: :international journal of aquatic biology 0
melika ghelichpour

effects of ambient copper was investigated on serum stress markers, sodium and enzyme levels in common carp ( cyprinus carpio l.) over a 14-d exposure period. fish were exposed to 0, 25 and 100 μg l -1 copper (as copper sulfate) and blood was sampled at 0, 3, 7 and 14 d after exposure. serum profile was significantly affected by copper concentration, sampling time and their interaction. increas...

Journal: :Dental materials journal 2007
Shogo Wakamatsu Takuji Ikemi

The aim of this study was to enhance the bond strength of one-step bonding agents to dentin. In particular, the focus was on using Catabrush the applicator system of AQ Bond Plus. Catabrush was supplemented with N-phenylglycine and aromatic sulfinate as polymerization accelerators, as N-phenylglycine was reportedly beneficial in improving the bond strength to dentin. The results indicated that ...

Journal: :The Journal of biological chemistry 1997
L Pollegioni W Blodig S Ghisla

The kinetic mechanism of the reaction of D-amino acid oxidase (EC 1.4.3.3) from Trigonopsis variabilis with [alpha-1H]- and [alpha-2H]phenylglycine has been determined. The pH dependence of Vmax is compatible with pKa values of approximately 8.1 and >9.5, the former of which is attributed to a base which should be deprotonated for efficient catalysis. The deuterium isotope effect on turnover is...

2006
D. Moslavac Forjan V. Vinković D. Kontrec

A new brush-type HPLC chiral stationary phase (CSP) comprising π-acidic N-(3,5-dinitrobenzoyl)-D-α-phenylglycine chiral units bound to the quinoxaline units of modified γ-aminopropyl silica gel by a 1,2-diaminoethane spacer has been prepared by solid-phase synthesis. To test the CSP attempts were made to separate the enantiomers of twenty-two racemates with different functional groups and the r...

2013
S.A. Zarubina I.V. Uporov E.A. Fedorchuk V.V. Fedorchuk A.V. Sklyarenko S.V. Yarotsky V.I. Tishkov

Alpha-amino acid ester hydrolase (EC 3.1.1.43, AEH) is a promising biocatalyst for the production of semi-synthetic β-lactam antibiotics, penicillins and cephalosporins. The AEH gene from Xanthomonas rubrilineans (XrAEH) was recently cloned in this laboratory. The three-dimensional structure of XrAEH was simulated using the homology modeling method for rational design experiments. The analysis ...

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