Results 141 to 150 of about 9,258 (171)
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The Structure of
The X-ray crystal structure of l-aspartate ammonia-lyase has been determined to 2.8 A resolution. The enzyme contains three domains, and each domain is composed almost completely of alpha helices. The central domain is composed of five long helices. In the tetramer, these five helices form a 20-helix cluster.
W, Shi +4 more
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Folia Microbiologica, 1988
Aspartate ammonia-lyase activity ofEscherichia alcalescens was positively affected by the composition of the culture medium and by a higher intensity of aeration. By using the supernatant obtained from autolyzed baker’s yeast, the aspartate ammonia-lyase activity increased two-fold (about 90 μkat/g wet biomass) as compared to commercial yeast ...
I. Pšenička +4 more
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Aspartate ammonia-lyase activity ofEscherichia alcalescens was positively affected by the composition of the culture medium and by a higher intensity of aeration. By using the supernatant obtained from autolyzed baker’s yeast, the aspartate ammonia-lyase activity increased two-fold (about 90 μkat/g wet biomass) as compared to commercial yeast ...
I. Pšenička +4 more
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Chemistry – A European Journal, 2013
Enzymatic amino acid synthesis: Kinetic resolution and asymmetric synthesis of various valuable 3-substituted aspartic acids, which were obtained in fair to good yields with diastereomeric ratio values of up to >98:2 and enantiomeric excess values of up to >99 %, by using engineered methylaspartate ammonia lyases are described.
Raj, Hans +8 more
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Enzymatic amino acid synthesis: Kinetic resolution and asymmetric synthesis of various valuable 3-substituted aspartic acids, which were obtained in fair to good yields with diastereomeric ratio values of up to >98:2 and enantiomeric excess values of up to >99 %, by using engineered methylaspartate ammonia lyases are described.
Raj, Hans +8 more
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Surface display of aspartate ammonia-lyase from Lactobacillus paracasei on Pichia pastoris
World Journal of Microbiology and BiotechnologyThis study explores the surface display of Lactobacillus paracasei aspartate ammonia-lyase (LpAAL) on Pichia pastoris using glycosylphosphatidylinositol (GPI) anchoring technology. LpAAL, an enzyme with broad substrate specificity, has significant potential in various industries, including food, pharmaceuticals, and cosmetics, due to its ability to ...
Chen-Chi, Chang +10 more
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Evaluation of Functionally Important Amino Acids in
The high-resolution structure of l-aspartate ammonia-lyase from Escherichia coli has recently been determined [Shi, W., Dunbar, J., Jayasekera, M. M. K., Viola, R. E., & Farber, G. K. (1997) Biochemistry 36, 9136-9144]. An examination of the putative active site has been carried out, with the active site located in a cleft that contains the ...
M M, Jayasekera +3 more
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Applied Biochemistry and Microbiology, 2015
Cloning of aspartase gene (L-aspartate ammonia-lyase) from the natural isolate Escherichia coli VKPM V-7188 in the pLATE31 plasmid composition and its expression under the control of the T7 phage promoter in Escherichia coli BLR (DE3) cells was performed. It was shown that the aspartase content in recombinant cells under optimal conditions is up to 60%
A. D. Novikov +5 more
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Cloning of aspartase gene (L-aspartate ammonia-lyase) from the natural isolate Escherichia coli VKPM V-7188 in the pLATE31 plasmid composition and its expression under the control of the T7 phage promoter in Escherichia coli BLR (DE3) cells was performed. It was shown that the aspartase content in recombinant cells under optimal conditions is up to 60%
A. D. Novikov +5 more
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Bioscience, Biotechnology, and Biochemistry, 1994
Four facultative anaerobes were isolated from soil as producers of 3-methylaspartate ammonia-lyase (MAL). They were identified as Citrobacter sp. No. 0504, Proteus sp. No. 0601, Escherichia coli No. 1002, and Enterobacter sp. No. 1202. The enzyme activities were induced when the strains were cultivated anaerobically or statically in the presence of (S)-
Y, Asano, Y, Kato
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Four facultative anaerobes were isolated from soil as producers of 3-methylaspartate ammonia-lyase (MAL). They were identified as Citrobacter sp. No. 0504, Proteus sp. No. 0601, Escherichia coli No. 1002, and Enterobacter sp. No. 1202. The enzyme activities were induced when the strains were cultivated anaerobically or statically in the presence of (S)-
Y, Asano, Y, Kato
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[Regulation of aspartate-ammonia-lyase (aspartase) biosynthesis in Pseudomonas fluorescens].
Biochimie, 1977Variations in aspartasic activity in various media are due to aspartate-ammonium lyase induction and to regulation of the biosynthesis of this enzyme. Evidence for neosynthesis of the enzyme is provided by labelling and separation of the protein. The inducer appears to be aspartic acid.
J C, Hubert, B, Wurtz
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[Isolation of spheroplasts from Escherichia coli 85 for aspartate-ammonia-lyase localization].
Prikladnaia biokhimiia i mikrobiologiia, 1988Conditions were determined for preparation of spheroplasts from E. coli under the action of lysozyme in the presence of EDTA. The preparation took from 10 to 15 min. The degree of conversion to spheroplasts was monitored spectrophotometrically at 660 nm.
V N, Shcherbakova +2 more
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Characterization and biocatalytic applications of aspartate and methylaspartate ammonia lyases
2012In zijn promotieonderzoek heeft Vinod Puthan Veetil het katalytische mechanisme van aspartaat ammonia lyase, dat lange tijd onbekend was, opgehelderd. Ook heeft hij het biokatalytische potentieel van een variant van methylaspartaat ammonia lyase benut voor de asymmetrische synthese van N-gesubstitueerde-L-aspartaatverbindingen. Aspartaat ammonia lyases
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