L-lactate dehydrogenase

This is an abbreviated version, for detailed information about L-lactate dehydrogenase, go to the full flat file.




A4-LDH, AdhE, anaerobic lactate dehydrogenase, BbLDH, dehydrogenase, lactate, eLDHA, eLDHB, Epsilon crystallin, epsilon-crystallin, H4-L-lactate dehydrogenase, heart LDH, Immunogenic protein p36, L(+)-nLDH, L-(+)-lactate dehydrogenase, L-lactate dehydrogenase B, L-lactic acid dehydrogenase, L-lactic dehydrogenase, L-LDH, lactate dehydrogenase, lactate dehydrogenase A, lactate dehydrogenase B, lactate dehydrogenase NAD-dependent, lactic acid dehydrogenase, lactic dehydrogenase, LctD, LDH, LDH-1, LDH-2, LDH-3, LDH-4, LDH-5, LDH-A, LDH-A4, LDH-m4, LDH1, LDH2, LdhA, LDHB, mLDH, More, muscle LDH, NAD-lactate dehydrogenase, nitric oxideinducible l-lactate dehydrogenase, PfLDH, proteins, specific or class, anoxic stress response, p34, Sa-LDH-1, TeLdhL, Tsac_0416


     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
       L-lactate dehydrogenase


Crystallization on EC - L-lactate dehydrogenase

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purified His-tagged wild-type and mutant H171C enzymes, hanging drop vapor diffusion method, 0.002 ml of 10 mg/ml protein in 20 mM Tris-HCl, pH 8.5, with 1 mM fructose 1,6-bisphosphate and NAD+, is mixed with 0.002 ml of reservoir solution containing 16% w/v PEG MME 2000, 0.06 M sodium/potassium phosphate, 1.8% v/v glycerol pH 5.5, or 14% w/v PEG 4000, 0.1 M sodium/potassium phosphate, 2% v/v glycerol, pH 7.0, equilibration against 1 ml reservoir solution, X-ray diffraction structure determinaation and analysis at 2.2-2.5 A resolution
apo enzyme form, X-ray diffraction structure determination and analysis at 2.35 A resolution, molecular replacement
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
crystal structure of a mutant into which an additional loop has been engineered in order to prevent tetramerization
binary complex of LDH with the cofactor NADH and the LDH/NADH-oxamate ternary complex, molecular dynamics, and simulation model from crystal structure at 2.1 A resolution, Protein DataBank entry 1IOZ, overview
overexpression in Escherichia coli
hanging drop method of vapour diffusion, ternary complex with NADH and oxamate
crystals the apo-form of PfLDH are ontained by hanging-drop method with 2-methyl-2,4-pentanediol as precipitant, crystallization of enzyme:naphthoic acid complexes with 2,6-naphthalenedicarboxalic acid, 2,6-naphthalene disulfonic acid or 3,7-dihydroxy naphthalene-2-carboxylic acid and 3,7-dihydroxy naphthalene-2-carboxylic acid plus NAD+
purified recombinant His-tagged Sa-LDH-1, sitting drop vapour diffusion method, 0.001 ml protein solution, containing 5 mg/ml protein in 20 mM Tris-HCl, 200 mM NaCl, pH 7.5, is mixed with mixed with an equal volume of reservoir solution, containing ,0.2 M calcium chloride dihydrate, 0.1 M Na HEPES, pH 7.5, 28%(v/v) PEG 400, and equilibrated against 0.1 ml reservoir solution, 3 days, X-ray diffraction structure determination and analysis at 2.4 A resolution
2.1 A resolution as a quarternary complex with the cofactor NADH, the allosteric activator fructose-1,6-bisphosphate and the substrate analog oxamate
apo enzyme form and enzyme in ternary complex, X-ray diffraction structure determination and analysis at 2.1-2.3 A resolution, molecular replacement
in apo-form and in ternary complexes containing NAD+ or NAD+-analogue 3-acetylpyridine adenine dinucleotide and sulfate or the inhibitor oxalate