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Literature summary for 1.1.1.27 extracted from

  • Nie, B.; Lodewyks, K.; Deng, H.; Desamero, R.Z.; Callender, R.
    Active-loop dynamics within the Michaelis complex of lactate dehydrogenase from Bacillus stearothermophilus (2016), Biochemistry, 55, 3803-3814.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.1.1.27

Activating Compound

Activating Compound Comment Organism Structure
fructose 1,6-bisphosphate assures that the protein forms tetrameric uniformity and serves as an allosteric activator of the enzyme Geobacillus stearothermophilus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten kinetic modelling, detailed overview. NADH can bind only to the open-loop apoenzyme, substrate analogue oxamate can bind only to the bsLDH·NADH binary complex in the open-loop conformation, and oxamate binding is followed by closing of the active site loop preventing oxamate unbinding. The open and closed states of the loop are in dynamic equilibrium and interconvert on the submillisecond time scale. This interconversion strongly accelerates with an increase in temperature because of significant enthalpy barriers. Binding of NADH to bsLDH results in minor changes of the loop dynamics and does not shift the open-closed equilibrium, but binding of the oxamate substrate mimic shifts this equilibrium to the closed state. At high excess oxamate concentrations where all active sites are nearly saturated with the substrate mimic, all active site mobile loops are mainly closed, kinetic analysis, overview Geobacillus stearothermophilus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(S)-lactate + NAD+ Geobacillus stearothermophilus
-
 pyruvate + NADH + H+
-
 r
pyruvate + NADH + H+ Geobacillus stearothermophilus
-
 (S)-lactate + NAD+
-
 r

Organism

Organism UniProt Comment Textmining
Geobacillus stearothermophilus P00344 i.e. Geobacillus stearothermophilus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-lactate + NAD+
-
 Geobacillus stearothermophilus pyruvate + NADH + H+
-
 r
additional information substrate analogue oxamate is isoelectric and isosteric to pyruvate and has binding kinetics very similar to that of pyruvate. As the substrate approaches the catalytic site, a catalytically key surface loop (residues 98-110) closes over the ligand, bringing residue Arg109 into hydrogen bonding contact with ligand, water leaves the pocket, and the pocket geometry rearranges to allow for favorable interactions between the cofactor and the ligand, which facilitates on-enzyme catalysis Geobacillus stearothermophilus ?
-
 ?
pyruvate + NADH + H+
-
 Geobacillus stearothermophilus (S)-lactate + NAD+
-
 r

Synonyms

Synonyms Comment Organism
lactate dehydrogenase
-
 Geobacillus stearothermophilus
LDH
-
 Geobacillus stearothermophilus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
20 40 assay at Geobacillus stearothermophilus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
 assay at Geobacillus stearothermophilus

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Geobacillus stearothermophilus
NADH kinetic modelling of NADH binding to the enzyme, overview Geobacillus stearothermophilus