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Literature summary extracted from

  • Antonyuk, S.V.; Strange, R.W.; Ellis, M.J.; Bessho, Y.; Kuramitsu, S.; Inoue, Y.; Yokoyama, S.; Hasnain, S.S.
    Structure of D-lactate dehydrogenase from Aquifex aeolicus complexed with NAD+ and lactic acid (or pyruvate) (2009), Acta Crystallogr. Sect. F, 65, 1209-1213.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.28 expression of D-LDH in Escherichia coli strain Rosetta (DE3) Aquifex aeolicus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.28 purified recombinant enzyme in fully closed formation with lactate or pyruvate bound to the active site of each subunit of the functional dimer, 0.001 ml of protein solution containing 20.3 mg/ml protein in 20 mM Tris-HCl buffer pH 8.0 containing 150 mM NaCl, is mixed with 0.001 ml of reservoir solution containing 0.1 M MES buffer, pH 6.0, and 25% w/v PEG 200, 10 days, method optimization, X-ray diffraction structure determination and analysis at 2.12 A resolution, molecular replacement and structure modelling Aquifex aeolicus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.28 D-lactate + NAD+ Aquifex aeolicus
-
 pyruvate + NADH
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.28 Aquifex aeolicus O66939
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.28 recombinant D-LDH from Escherichia coli strain Rosetta (DE3) by ultracentrifugation, anion exchange and hydroxyapatite chromatography, followed by gel filtration Aquifex aeolicus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.28 D-lactate + NAD+
-
 Aquifex aeolicus pyruvate + NADH
-
 r
1.1.1.28 D-lactate + NAD+ during oxidation of NADH to NAD+, NADH transfers a hydride ion to pyruvate, in the reverse reaction NAD+ receives a hydride ion from lactate, D-lactate binding structure, overview Aquifex aeolicus pyruvate + NADH pyruvate binding structure, overview r
1.1.1.28 additional information each subunit of the homodimer in a closed conformation binds NADH to the coenzyme-binding domain and a lactate or pyruvate molecule at the interdomain active-site cleft, structure, overview Aquifex aeolicus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.1.28 dimer biologically significant unit in the D-LDH enzymes is probably a homodimer Aquifex aeolicus

Synonyms

EC Number Synonyms Comment Organism
1.1.1.28 D-LDH
-
 Aquifex aeolicus

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.28 additional information cofactor binding structure, each subunit of the homodimer in a closed conformation binds the NADH cofactor to the coenzyme-binding domain Aquifex aeolicus
1.1.1.28 NAD+
-
 Aquifex aeolicus
1.1.1.28 NADH
-
 Aquifex aeolicus

General Information

EC Number General Information Comment Organism
1.1.1.28 evolution two evolutionarily distinct families of LDH enzymes perform the oxidation of NADH/reduction of NAD+ to yield a product that differs only in its chirality: L-lactate or D-lactate Aquifex aeolicus