Results 271 to 280 of about 312,266 (316)
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D- and L-lactate dehydrogenases in Escherichia coli
Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation, 1966Summary (1) The oxidation of DL -lactate by Escherichia coli NCTC 8196 has been shown to be catalysed by two enzymes, one specific for D -lactate, the other specific for L -lactate. (2) Both enzymes were present during aerobic and anaerobic growth on all media tested.
A. Hurst, R. Bennett, D.R. Taylor
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Preparative affinity precipitation of L-lactate dehydrogenase
Journal of Biotechnology, 1989Abstract The methoxylated p-sulphonate isomer of the triazine dye C.I. Reactive Blue 2, selectively precipitates L-lactate dehydrogenase from crude rabbit muscle extracts. At mildly alkaline pH values and a 7-fold molar excess of the dye analogue to enzyme subunits, 106 mg of homogeneous lactate dehydrogenase essentially free of soluble ligands and ...
James C. Pearson +2 more
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Mechanism of allosteric transition of bacterial L-lactate dehydrogenase
Faraday Discussions, 1992The allosteric behaviour of L-lactate dehydrogenase (L-lactate:NAD+oxidoreductase, EC 1.1.1.27, LDH) from Bifidobacterium longum aM101-2 was studied by means of the subunit hybridization technique as well as X-ray crystallography. Homotropic allosteric response of the LDH activity was found against the concentration of its substrate, pyruvate ...
So Iwata +3 more
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Low resolution study of crystalline l-lactate dehydrogenase
Journal of Molecular Biology, 1969The electron density distribution of dogfish muscle lactate dehydrogenase, based on 2000 independent terms extending to 5 A resolution, shows the shape of the tetrameric molecule and of the individual subunits. Each of the five heavy-atom derivatives used in the calculation substitutes at one or more of three sites A, B and C. The heavy-atom compounds (
Michael G. Rossmann +7 more
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Journal of Biochemistry (Tokyo), 1982
Heat-stable L-lactate dehydrogenase [EC 1.1.1.27] was purified from an extremely thermophilic bacterium belonging to the genus Thermus, and it showed an allosteric nature dependent on fructose 1,6-bisphosphate as an effector.
H. Taguchi +3 more
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Heat-stable L-lactate dehydrogenase [EC 1.1.1.27] was purified from an extremely thermophilic bacterium belonging to the genus Thermus, and it showed an allosteric nature dependent on fructose 1,6-bisphosphate as an effector.
H. Taguchi +3 more
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Journal of Biotechnology, 2009
D-form lactate is often found in fermented foods and excessive dietary intake of D-lactate may cause metabolic stress in both infants and patients. Leuconostoc citreum is a major lactic acid bacterium that produces D-lactate in fermented foods. The aim of this study was to change the pyruvate carbon flux in L.
Hyun-Ju Eom +6 more
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D-form lactate is often found in fermented foods and excessive dietary intake of D-lactate may cause metabolic stress in both infants and patients. Leuconostoc citreum is a major lactic acid bacterium that produces D-lactate in fermented foods. The aim of this study was to change the pyruvate carbon flux in L.
Hyun-Ju Eom +6 more
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Molecular Basis of Allosteric Activation of Bacterial L-Lactate Dehydrogenase
Journal of Molecular Biology, 1993The three-dimensional structure of allosteric L-lactate dehydrogenase from Bifidobacterium longum, the first example of a T-state structure of L-lactate dehydrogenase, has been determined to 2.0 A. A comparative study of this structure with the previously reported R-state structure from Bacillus stearothermophilus has revealed the allosteric activation
Takahisa Ohta, So Iwata
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L(+)‐lactate dehydrogenases from Hymenolepis diminuta (Cestoda)
Journal of Experimental Zoology, 1973AbstractProperties of L( + )‐lactate dehydrogenases from infective eggs, cysticercoids, immature proglottids (anteriors), and pre‐patent (seven day) infections of H. diminuta were studied. Fractionation of isozymes by disc gel and cellulose acetate electrophoresis was unsatisfactory, but some fractionation was obtained by electrofocusing.
Donald Fairbairn, Michael Walkey
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The complete primary structure of the allosteric L-lactate dehydrogenase from Lactobacillus casei.
European Journal of Biochemistry, 1983The polypeptide chain of the allosteric L-lactate dehydrogenase (EC 1.1.1.27) of Lactobacillus casei consists of 325 amino acid residues. Despite the strikingly different enzymatic characteristics of the allosteric L-lactate dehydrogenase of L. casei and
R. Hensel, U. Mayr, C. Yang
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Cloning and characterization of l-lactate dehydrogenase gene of Staphylococcus aureus
Anaerobe, 2013Staphylococcus aureus a natural inhabitant of nasopharyngeal tract survives in the host as biofilms. In the present study S. aureus ATCC12600 grown under anaerobic conditions showed biofilm units of 0.086 as compared to 0.07 when this pathogen grown in aerobic conditions with elevated lactate formation and the same was also observed with increased ...
Uppu Venkateswara Prasad +5 more
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