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Literature summary for 1.1.1.27 extracted from

  • Zhao, R.; Zheng, S.; Duan, C.; Liu, F.; Yang, L.; Huo, G.
    NAD-dependent lactate dehydrogenase catalyses the first step in respiratory utilization of lactate by Lactococcus lactis (2013), FEBS Open Bio, 3, 379-386.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.1.1.27

Activating Compound

Activating Compound Comment Organism Structure
D-fructose-1,6-bisphophate FBP, L-nLDH activity is FBP dependent Lactococcus cremoris

Cloned(Commentary)

Cloned (Comment) Organism
gene ldh, recombinant expression of C-terminally His-tagged enzyme in Escherichia coli strain M15 Lactococcus cremoris

Inhibitors

Inhibitors Comment Organism Structure
ADP ADP is a more severe inhibitor and has a more severe inhibitory effect on the lactate oxidation reaction. But its relative inhibition on reverse reactions is weak at low ADP concentrations Lactococcus cremoris
ATP inhibitory effects of ATP on both directions are weak and similar as both rates remain above 80% in the presence of 8 mM ATP Lactococcus cremoris
Lactate a high concentration of lactate has a weak inhibitory effect on the pyruvate reduction reaction activity but is meaningful for a significant lactate oxidation rate as the K m value of LDHA for L-lactate is very high Lactococcus cremoris

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information enzyme kinetics, ordered bi–bi kinetic mechanism of nLDH with the coenzyme binding first Lactococcus cremoris
0.066
-
 NADH pH 7.0, 30°C, recombinant enzyme, with 1 mM D-fructose-1,6-bisphophate Lactococcus cremoris
0.38
-
 NAD+ pH 7.0, 30°C, recombinant enzyme, with 1 mM D-fructose-1,6-bisphophate Lactococcus cremoris
1.95
-
 pyruvate pH 7.0, 30°C, recombinant enzyme, with 1 mM D-fructose-1,6-bisphophate Lactococcus cremoris
158
-
 (S)-lactate pH 7.0, 30°C, recombinant enzyme, with 1 mM D-fructose-1,6-bisphophate Lactococcus cremoris

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(S)-lactate + NAD+ Lactococcus cremoris lactate oxidation does not occur unless pyruvate and especially NADH drop to low levels pyruvate + NADH + H+
-
 r
(S)-lactate + NAD+ Lactococcus cremoris MG1363 lactate oxidation does not occur unless pyruvate and especially NADH drop to low levels pyruvate + NADH + H+
-
 r
pyruvate + NADH + H+ Lactococcus cremoris
-
 (S)-lactate + NAD+
-
 r
pyruvate + NADH + H+ Lactococcus cremoris MG1363
-
 (S)-lactate + NAD+
-
 r

Organism

Organism UniProt Comment Textmining
Lactococcus cremoris
-
-
-
Lactococcus cremoris MG1363
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant C-terminally His-tagged enzyme from Escherichia coli strain M15 by nickel affinity chromatography Lactococcus cremoris

Reaction

Reaction Comment Organism Reaction ID
(S)-lactate + NAD+ = pyruvate + NADH + H+ the enzyme LDHA shows an ordered bi–bi kinetic mechanism of nLDH with the coenzyme binding first Lactococcus cremoris
a

Source Tissue

Source Tissue Comment Organism Textmining
cell culture FBP-activated L-nLDH activity is constantly very significant throughout the growth period, even when lactate is consumed in the stationary phase of respiration. During the lactate utilization period, L-nLDH activity is regulated by some factors and the pyruvate reduction activity is completely inhibited or masked Lactococcus cremoris
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
9.3 12.2 native enzyme in strain MG1363 at different growth phases and conditions, pH 7.0, 30°C Lactococcus cremoris

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-lactate + NAD+
-
 Lactococcus cremoris pyruvate + NADH + H+
-
 r
(S)-lactate + NAD+ lactate oxidation does not occur unless pyruvate and especially NADH drop to low levels Lactococcus cremoris pyruvate + NADH + H+
-
 r
(S)-lactate + NAD+
-
 Lactococcus cremoris MG1363 pyruvate + NADH + H+
-
 r
(S)-lactate + NAD+ lactate oxidation does not occur unless pyruvate and especially NADH drop to low levels Lactococcus cremoris MG1363 pyruvate + NADH + H+
-
 r
pyruvate + NADH + H+
-
 Lactococcus cremoris (S)-lactate + NAD+
-
 r
pyruvate + NADH + H+
-
 Lactococcus cremoris MG1363 (S)-lactate + NAD+
-
 r

Synonyms

Synonyms Comment Organism
L-nLDH
-
 Lactococcus cremoris
LDH
-
 Lactococcus cremoris
LdhA
-
 Lactococcus cremoris
NAD-dependent lactate dehydrogenase
-
 Lactococcus cremoris

Temperature Optimum [°C]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Lactococcus cremoris

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Lactococcus cremoris
NADH
-
 Lactococcus cremoris

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
additional information
-
 additional information inhibition kinetics Lactococcus cremoris

General Information

General Information Comment Organism
evolution genes ldh, ldhB and ldhX, are transcribed to some extent in Lactococcus lactis strain MG1363. The product of the ldhX gene has little nLDH activity as well as ldhB which exhibits only leaky transcription and plays a minor role in lactate yield. LDHA encoded by ldh has been found to perform major L-nLDH activity, with the contribution of other alternate L-nLDHs being small Lactococcus cremoris
metabolism NAD-dependent lactate dehydrogenase catalyses the first step in respiratory utilization of lactate by Lactococcus lactis Lactococcus cremoris