Zobrazeno 1 - 10
of 13
pro vyhledávání: '"V. K. Svedas"'
Publikováno v:
Acta Naturae
Until recently, the biocatalytic preparation of enantiomerically pure amines was based on stereoselective acyl transfer in an organic medium using activated acyl donors. The possibility of performing an effective and enantioselective enzymatic acylat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::e4ed6deece122be45019ac93192106b7
https://pubmed.ncbi.nlm.nih.gov/22649633
https://pubmed.ncbi.nlm.nih.gov/22649633
Publikováno v:
Acta Naturae
Hsp70 is a chaperone protein that participates in the folding of de novo synthesized proteins, protection of the hydrophobic regions of denaturated proteins, the regulation of apoptosis, the immune response, and several other cellular processes. Desp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::e2490d17e194879bfdd557e398597ebf
https://pubmed.ncbi.nlm.nih.gov/22649666
https://pubmed.ncbi.nlm.nih.gov/22649666
Publikováno v:
Acta Naturae
A bioinformatic and phylogenetic study has been performed on a family of penicillin–binding proteins including D–aminopeptidases, D–amino acid amidases, DD–carboxypeptidases, and β –lactamases. Significant homology between D–aminopeptida
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::56678aa88b9338691b15dcf0f102d139
https://pubmed.ncbi.nlm.nih.gov/22649642
https://pubmed.ncbi.nlm.nih.gov/22649642
Publikováno v:
Biochemistry. Biokhimiia. 68(3)
The influence of the external nucleophile (6-aminopenicillanic acid) on the kinetics of the penicillin acylase-catalyzed acyl transfer reactions was studied using a highly sensitive spectrophotometric assay. An adequate kinetic scheme is suggested ba
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::fd83d81897b82fc75c4247bfa8e33243
https://pubmed.ncbi.nlm.nih.gov/12733976
https://pubmed.ncbi.nlm.nih.gov/12733976
Autor:
M I, Youshko, V K, Svedas
Publikováno v:
Biochemistry. Biokhimiia. 65(12)
Kinetic regularities of the enzymatic acyl group transfer reactions have been studied using ampicillin synthesis catalyzed by E. coli penicillin acylase as an example. It was shown that ampicillin synthesis proceeds through the formation of an acylen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::4a91215c3127bb6e43dda3c3a303b153
https://pubmed.ncbi.nlm.nih.gov/11173507
https://pubmed.ncbi.nlm.nih.gov/11173507
Publikováno v:
Biochemistry. Biokhimiia. 65(8)
Inhibition of penicillin acylases from Escherichia coli and Alcaligenes faecalis by aliphatic and aromatic alcohols was studied. It was shown that the inhibition of both enzymes has competitive nature and they bind the alcohols at the acyl group bind
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::54691801e5e50e0fd11bb04c76120aa0
https://pubmed.ncbi.nlm.nih.gov/11002191
https://pubmed.ncbi.nlm.nih.gov/11002191
Autor:
T A, Shamolina, V K, Svedas
Publikováno v:
Biochemistry. Biokhimiia. 65(6)
Individual subunits of penicillin acylase from E. coli were isolated by gel-filtration under denaturing conditions (8 M urea). Recovery of the catalytic activity of the penicillin acylase heterodimer was studied after removal of urea. In the case of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::bc7f673c7c648b28ded9cba42ab2a8bb
https://pubmed.ncbi.nlm.nih.gov/10887285
https://pubmed.ncbi.nlm.nih.gov/10887285
Publikováno v:
Biochemistry. Biokhimiia. 64(10)
The behavior of a penicillin acylase from E. coli was studied in the reversed-micelle system AOT--H2O--octane. Kinetic studies of the enzymatic hydrolysis of the m-carboxy-p-nitroanilide of phenylacetic acid, titration of the penicillin acylase activ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::bffdbf8df0e88d80d079317d3658f7dc
https://pubmed.ncbi.nlm.nih.gov/10561567
https://pubmed.ncbi.nlm.nih.gov/10561567
Publikováno v:
Biochemistry. Biokhimiia. 64(10)
Stability and catalytic properties of native and immobilized penicillin acylase were studied in systems with low water content. Preparations of both native and immobilized penicillin acylase demonstrated the catalytic activity even in solid-phase sys
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::edca7afbb2fc452efe7ebf35ea867253
https://pubmed.ncbi.nlm.nih.gov/10561568
https://pubmed.ncbi.nlm.nih.gov/10561568
Publikováno v:
Biochemistry. Biokhimiia. 63(9)
Penicillin acylase substrates suitable for colorimetric determination of the enzyme activity have been tested in this study. The kinetic parameters (Km and kcat) have been elucidated for the following nine substrates: six phenylacetic acid derivative
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::fc8e3a2072248c7601ad9dfdd6c6c1ee
https://pubmed.ncbi.nlm.nih.gov/9795283
https://pubmed.ncbi.nlm.nih.gov/9795283