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Literature summary for 1.1.1.27 extracted from

  • Gaspar, P.; Neves, A.R.; Shearman, C.A.; Gasson, M.J.; Baptista, A.M.; Turner, D.L.; Soares, C.M.; Santos, H.
    The lactate dehydrogenases encoded by the ldh and ldhB genes in Lactococcus lactis exhibit distinct regulation and catalytic properties - comparative modeling to probe the molecular basis (2007), FEBS J., 274, 5924-5936.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
D-fructose 1,6-bisphosphate activation constants of isozymes at different pH values, overview Lactococcus lactis

Cloned(Commentary)

Cloned (Comment) Organism
genes ldh and ldhB, sequence determination, analysis, and comparison Lactococcus lactis

Protein Variants

Protein Variants Comment Organism
additional information construction of an ldh gene insertion mutant strain FI9078, the insertion of an IS905-like element, that created a hybrid promoter in the intergenic region upstream of ldhB, leads to activation of a second isozyme LDHB, which shows a strongly pH-dependent activity, overview Lactococcus lactis

Inhibitors

Inhibitors Comment Organism Structure
phosphate phosphate acts as a strong activator of LDHB Lactococcus lactis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information isozymes LDH and LDHB, kinetic analysis, NADH saturation curves of LDHB become more sigmoidal with increasing pH from pH 5.5 to pH 7.2, resulting in a marked decrease of the affinity for this cofactor, while the Km of LDH for NADH does not change with pH Lactococcus lactis
0.054
-
NADH pH 6.0, 30°C, isozyme LDH Lactococcus lactis
0.058
-
NADH pH 7.0, 30°C, isozyme LDH Lactococcus lactis
0.077
-
NADH pH 6.0, 30°C, isozyme LDHB Lactococcus lactis
0.364
-
NADH pH 7.0, 30°C, isozyme LDHB Lactococcus lactis
1.3
-
pyruvate pH 6.0, 30°C, isozyme LDHB Lactococcus lactis
1.5
-
pyruvate pH 6.0, 30°C, isozyme LDH Lactococcus lactis
1.7
-
pyruvate pH 7.0, 30°C, isozyme LDH Lactococcus lactis
2.9
-
pyruvate pH 7.0, 30°C, isozyme LDHB Lactococcus lactis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(S)-lactate + NAD+ Lactococcus lactis LDH is a key enzyme in homolactic fermentation catalyzing the reduction of pyruvate to lactate with the concomitant oxidation of NADH, LDH and LDHB are involved in glycolysis pyruvate + NADH + H+
-
r
(S)-lactate + NAD+ Lactococcus lactis MG1363 LDH is a key enzyme in homolactic fermentation catalyzing the reduction of pyruvate to lactate with the concomitant oxidation of NADH, LDH and LDHB are involved in glycolysis pyruvate + NADH + H+
-
r
additional information Lactococcus lactis intracellular isozyme regulation in relation to pH, overview ?
-
?
additional information Lactococcus lactis MG1363 intracellular isozyme regulation in relation to pH, overview ?
-
?

Organism

Organism UniProt Comment Textmining
Lactococcus lactis P0C2T6 genes ldh and ldhB
-
Lactococcus lactis MG1363 P0C2T6 genes ldh and ldhB
-

Purification (Commentary)

Purification (Comment) Organism
isozymes LDHB and LDH 400fold and 30fold, from cell extracts of strains FI9078 and MG1363, respectively Lactococcus lactis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-lactate + NAD+ LDH is a key enzyme in homolactic fermentation catalyzing the reduction of pyruvate to lactate with the concomitant oxidation of NADH, LDH and LDHB are involved in glycolysis Lactococcus lactis pyruvate + NADH + H+
-
r
(S)-lactate + NAD+ LDH posseses a catalytic His171 residue Lactococcus lactis pyruvate + NADH + H+
-
r
(S)-lactate + NAD+ LDH is a key enzyme in homolactic fermentation catalyzing the reduction of pyruvate to lactate with the concomitant oxidation of NADH, LDH and LDHB are involved in glycolysis Lactococcus lactis MG1363 pyruvate + NADH + H+
-
r
(S)-lactate + NAD+ LDH posseses a catalytic His171 residue Lactococcus lactis MG1363 pyruvate + NADH + H+
-
r
additional information intracellular isozyme regulation in relation to pH, overview Lactococcus lactis ?
-
?
additional information intracellular isozyme regulation in relation to pH, overview Lactococcus lactis MG1363 ?
-
?

Subunits

Subunits Comment Organism
More LDH has a slightly larger negative charge than LDHB and a greater concentration of positive charges at the interface between monomers Lactococcus lactis

Synonyms

Synonyms Comment Organism
LDH
-
Lactococcus lactis
LDHB
-
Lactococcus lactis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Lactococcus lactis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5 6 isozyme LDHB Lactococcus lactis

pH Range

pH Minimum pH Maximum Comment Organism
additional information
-
the two isozymes LDH and LDHB exhibited different pH profiles for maximal activity Lactococcus lactis
5.2 7.2 LDH activity shows a broad plateau between pH 5.2 and pH 7.2, and no activity at pH 4.8 Lactococcus lactis

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Lactococcus lactis
NADH NADH saturation curves of LDHB become more sigmoidal with increasing pH from pH 5.5 to pH 7.2, resulting in a marked decrease of the affinity for this cofactor, while the Km of LDH for NADH did not change with pH Lactococcus lactis

pI Value

Organism Comment pI Value Maximum pI Value
Lactococcus lactis isozyme LDH, sequence calculation
-
4.9
Lactococcus lactis isozyme LDHB, sequence calculation
-
5.2