1.1.1.27: L-lactate dehydrogenase

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

Reaction

(S)-lactate
+
NAD+
=
pyruvate
+
NADH
+
H+

Synonyms

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, L-lactate dehydrogenase B, L-lactic acid dehydrogenase, L-lactic dehydrogenase, L-LDH, L-nLDH, lactate dehydrogenase, lactate dehydrogenase 5, 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, ldhL, mLDH, More, muscle LDH, NAD-dependent lactate dehydrogenase, NAD-lactate dehydrogenase, nitric oxideinducible l-lactate dehydrogenase, PfLDH, proteins, specific or class, anoxic stress response, p34, Sa-LDH-1, SMU.1115, SMU_1115, TeLdhL, Tsac_0416

ECTree

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

Crystallization

Crystallization on EC 1.1.1.27 - L-lactate dehydrogenase

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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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 recombinant enzyme as apo-enzyme and in four ternary complexes, The ternary complexes capture the enzyme bound to NAD/NADH or its 3-acetylpyridine analogue in the cofactor binding pocket, while the substrate binding site is occupied by one of the following ligands: lactate, pyruvate or oxamate. X-ray diffraction structure determination and analysis at 2.0-2.3 A resolution
-
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
purified recombinant wild-type enzyme, in apoform and in complex with fructose-1,6-bisphosphate and NADH, X-ray diffraction structure determination and analysis at 2.38 A and 2.30 A resolution, respectively, modelling
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
-
lactate dehydrogenase A in apo form, in ternary complex with oxalate and kanamycin, and in inhibitor-bound form, hanging drop vapour diffusion method, apo-LDHA crystals are grown by mixing of 0.002 ml of 25 mg/ml enzyme protein with 0.002 ml reservoir solution consisting of 100 mM Bis-Tris propane, pH 7.0, 20% v/v PEG 400, and 100 mM LiCl. LDHA-NADH crystals are grown by first incubating 25 mg/ml enzyme protein with 3 mM NADH for 2 h at 4C and then setting up 0.004 ml drops with a 2:1:1 volume ratio of LDHA-NADH, reservoir solution, containing 18% w/v PEG 3350, and 50 mM HEPES, pH 6.8, and another reagent containing 0.16% w/v L-citrulline, 0.16% w/v L-ornithine hydrochloride, 0.16% w/v urea, 0.16% w/v oxalic acid, 0.16% w/v kanamycin monosulfate, and 0.16% w/v L-arginine in 0.02 M HEPES sodium, pH 6.8, 20C. Apo and NADH-bound LDHA crystals appear after three weeks. LDHA-inhibitor complex crystals are obtained by adding 0.010 ml soaking solution containing 20 mM inhibitor, 100 mM HEPES, pH 7.5, 50 mM LiCl, 100 mM bis-tris propane pH 7.0, 20% v/v DMSO, and 25% PEG 8000, to 0.002 ml hanging drops containing apo LDHA crystals and allowing the crystals to sit at room temperature for 24 h, X-ray diffraction structure determination and analysis at 2.1-3.2 A resolution, molecular replacement method using model structure PDB ID1i10
-
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
-