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EC Tree
IUBMB Comments Also oxidizes other (S)-2-hydroxymonocarboxylic acids. NADP+ also acts, more slowly, with the animal, but not the bacterial, enzyme.
The taxonomic range for the selected organisms is: Deinococcus radiodurans The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
lactate dehydrogenase, lactic dehydrogenase, ldh-a, lactate dehydrogenase a, l-lactate dehydrogenase, ldh-5, lactic acid dehydrogenase, ldh-1, pfldh, alpha-hydroxybutyrate dehydrogenase,
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dehydrogenase, lactate
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Epsilon crystallin
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epsilon-crystallin
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Immunogenic protein p36
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L-(+)-lactate dehydrogenase
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L-lactic acid dehydrogenase
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L-lactic dehydrogenase
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lactate dehydrogenase
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lactate dehydrogenase NAD-dependent
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lactic acid dehydrogenase
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lactic dehydrogenase
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NAD-lactate dehydrogenase
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proteins, specific or class, anoxic stress response, p34
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(S)-lactate:NAD+ oxidoreductase
Also oxidizes other (S)-2-hydroxymonocarboxylic acids. NADP+ also acts, more slowly, with the animal, but not the bacterial, enzyme.
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pyruvate + NADH + H+
(S)-lactate + NAD+
pyruvate + NADH + H+
(S)-lactate + NAD+
LDH catalyzes the conversion of pyruvate to lactate with concomitant oxidation of NADH during the last step in anaerobic glycolysis
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r
pyruvate + NADH + H+
(S)-lactate + NAD+
active site structure and substrate binding, overview
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r
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pyruvate + NADH + H+
(S)-lactate + NAD+
LDH catalyzes the conversion of pyruvate to lactate with concomitant oxidation of NADH during the last step in anaerobic glycolysis
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r
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additional information
thermodynamic activation parameters, overview
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additional information
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thermodynamic activation parameters, overview
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0.21
pyruvate
pH 7.0, 0°C, recombinant enzyme
additional information
additional information
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additional information
additional information
an allosteric enzyme
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additional information
additional information
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an allosteric enzyme
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884
pyruvate
pH 7.0, 0°C, recombinant enzyme
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7
the enzyme shows a narrow pH optimum
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additional information
pH profile
additional information
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pH profile
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Uniprot
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additional information
structural features for structural stability, comparison to enzymes from other species in extreme environments
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additional information
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structural features for structural stability, comparison to enzymes from other species in extreme environments
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additional information
primary sequence, tertiary structure modelling, analysis of the apo form and ternary complexes from crystal structure, overview
additional information
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primary sequence, tertiary structure modelling, analysis of the apo form and ternary complexes from crystal structure, overview
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purified enzyme, hanging drop vapor diffusion technique, 8 mg/ml protein in 20% PEG 5000 MME, 0.1M bicine, pH 9.0, at room temperature, X-ray diffraction structure determination and analysis at 2.5 A resolution, molecular replacement
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60
stable up to, thermal stability in relation to enzyme structure comparison to enzymes from other species in extreme environments
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recombinant enzyme from Escherichia coli strain DH5alpha by heat treatment at 55°C for 90 s, hydrophobic interaction chromatography, hydroxyapatite chromatography, gel filtration, and ultrafiltration
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expression in Escherichia coli strain DH5alpha
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Coquelle, N.; Fioravanti, E.; Weik, M.; Vellieux, F.; Madern, D.
Activity, stability and structural studies of lactate dehydrogenases adapted to extreme thermal environments
J. Mol. Biol.
374
547-562
2007
Champsocephalus gunnari (O93541), Champsocephalus gunnari, Deinococcus radiodurans (P50933), Deinococcus radiodurans, Thermus thermophilus (Q5SJA1), Thermus thermophilus
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