Literature summary for 1.1.1.28 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.

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Crystallization (Comment)

Organism

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)

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

Organism

Organism	UniProt	Comment	Textmining
Aquifex aeolicus	O66939	-	-

Purification (Commentary)

Purification (Comment)	Organism
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)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
D-lactate + NAD+	-	Aquifex aeolicus	pyruvate + NADH	-	r
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
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

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

Synonyms

Synonyms	Comment	Organism
D-LDH	-	Aquifex aeolicus

Cofactor

Cofactor	Comment	Organism
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
NAD+	-	Aquifex aeolicus
NADH	-	Aquifex aeolicus

General Information

General Information	Comment	Organism
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