Results 131 to 140 of about 9,258 (171)

L-aspartate ammonia-lyase and fumarate hydratase share extensive sequence homology

Biochemical and Biophysical Research Communications, 1986
Based on our recent determinations of the nucleotide sequences of the L-aspartate ammonia-lyase genes from Escherichia coli and Pseudomonas fluorescens, primary structures of the two L-aspartate ammonia-lyases and fumarate hydratases from Bacillus subtilis and E. coli (N-terminal partial sequence) were compared by computer analysis.
J S, Takagi, M, Tokushige, Y, Shimura, M, Kanehisa   +3 more
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A QM/MM study of the catalytic mechanism of aspartate ammonia lyase

Journal of Molecular Graphics and Modelling, 2014
Aspartate ammonia lyase (Asp) is one of three types of ammonia lyases specific for aspartate or its derivatives as substrates, which catalyzes the reversible reaction of l-aspartate to yield fumarate and ammonia. In this paper, the catalytic mechanism of Asp has been studied by using combined quantum-mechanical/molecular-mechanical (QM/MM) approach ...
Jing, Zhang, Yongjun, Liu
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Immobilized l-aspartate ammonia-lyase from Bacillus sp. YM55-1 as biocatalyst for highly concentrated l-aspartate synthesis

Bioprocess and Biosystems Engineering, 2012
L-aspartate ammonia-lyase from Bacillus sp. YM55-1 (AspB, EC 4.3.1.1) catalyzes the reversible conversion of L-aspartate (Asp) into fumarate and ammonia with a high specific activity toward the substrate. AspB was expressed in Escherichia coli and partially purified by heat precipitation and saturation with ammonium sulfate reaching purification factor
Max, Cárdenas-Fernández, Carmen, López, Gregorio, Alvaro, Josep, López-Santín   +3 more
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Bioproduction of l-Aspartic Acid and Cinnamic Acid by l-Aspartate Ammonia Lyase from Pseudomonas aeruginosa PAO1

Applied Biochemistry and Biotechnology, 2016
Aspartase (L-aspartate ammonia lyase, EC 4.3.1.1) catalyses the reversible amination and deamination of L-aspartic acid to fumaric acid which can be used to produce important biochemical. In this study, we have explored the characteristics of aspartase from Pseudomonas aeruginosa PAO1 (PA-AspA).
Arti T, Patel, Rekha C, Akhani, Manisha J, Patel, Samir R, Dedania, Darshan H, Patel   +4 more
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Genetically modifying aspartate aminotransferase and aspartate ammonia-lyase affects metabolite accumulation in l-lysine producing strain derived from Corynebacterium glutamicum ATCC13032

Journal of Molecular Catalysis B: Enzymatic, 2015
Abstract The aspartate aminotransferase (AAT) and aspartate ammonia-lyase (AAL) catalyzes respectively the reversible reaction of oxaloacetate (OAA) and fumarate to form l -aspartate. However, the effects of AAT and AAL on metabolite variations have not been clearly elucidated as yet.
Jianzhong Xu, Junlan Zhang, Yanfeng Guo, Weiguo Zhang   +3 more
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Catalytic Mechanisms and Biocatalytic Applications of Aspartate and Methylaspartate Ammonia Lyases

ACS Chemical Biology, 2012
Ammonia lyases catalyze the formation of α,β-unsaturated bonds by the elimination of ammonia from their substrates. This conceptually straightforward reaction has been the emphasis of many studies, with the main focus on the catalytic mechanism of these enzymes and/or the use of these enzymes as catalysts for the synthesis of enantiomerically pure α ...
Marianne, de Villiers, Vinod, Puthan Veetil, Hans, Raj, Jandré, de Villiers, Gerrit J, Poelarends   +4 more
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Structural Basis for the Catalytic Mechanism of Aspartate Ammonia Lyase

Biochemistry, 2011
Aspartate ammonia lyases (or aspartases) catalyze the reversible deamination of L-aspartate into fumarate and ammonia. The lack of crystal structures of complexes with substrate, product, or substrate analogues so far precluded determination of their precise mechanism of catalysis. Here, we report crystal structures of AspB, the aspartase from Bacillus
Fibriansah, Guntur, Veetil, Vinod Puthan, Poelarends, Gerrit J., Thunnissen, Andy-Mark W. H.   +3 more
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Effect of detergents on aspartate ammonia-lyase activity inEscherichia alcalescens

Folia Microbiologica, 1988
The effect of twelve detergents on aspartate ammonia-lyase activity of Escherichia alcalescens used for the production of L-aspartic acid was tested. Best permeabilization was found with Triton X-100, Slovafol 910 and Corona, a mixed commercial preparation.
V, Malaník, M, Malaníková, I, Psenicka, I, Sojková, M, Marek   +4 more
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Magnetically agitated continuous-flow tube reactors with aspartate ammonia-lyase immobilized on magnetic nanoparticles

Reaction Chemistry & Engineering, 2023
Continuous-flow tube reactors agitating the aspartate ammonia-lyase on magnetic nanoparticles by two external permanent magnets within the reaction stream showed AAL-MNPs being the most efficient in the rotating magnets system.
Ali O. Imarah, Fausto M. W. G. Silva, Naran Bataa, Balázs Decsi, Diána Balogh-Weiser, László Poppe   +5 more
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Immobilization of Escheria alcalescens cells with aspartate ammonia-lyase activity

Biotechnology Letters, 1988
Immobilization of Escherichia alcalescens cells into genu-carrageenan gel for L-aspartic acid production was studied with respect to the optimized preparation of heterogenous biocatalyst /2.5–3.0% genu-carrageenan, 15% biomass, 50–55 °C, tannin added/.
M. Malaníková, V. Malaník, I. Pšenička, M. Marek   +3 more
openaire   +1 more source