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Literature summary for 1.1.1.27 extracted from

  • Goto, T.; Sugawara, K.; Nakamura, S.; Kidokoro, S.I.; Wakui, H.; Nunomura, W.
    Enzymatic and thermodynamic profiles of a heterotetramer lactate dehydrogenase isozyme in swine (2016), Biochem. Biophys. Res. Commun., 479, 860-867.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
in somatic cells, LDH forms homotetramers and heterotetramers that are encoded by two different genes: LDHA (skeletal muscle type, M) and LDHB (heart type, H) Sus scrofa

Inhibitors

Inhibitors Comment Organism Structure
hydroxychloroquine
-
Sus scrofa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Michaelis-Menten and Hanes-Woolf kinetic analysis and thermodynamics of isozymes H4, M4, and H2M2, overview. The Km values for heteroterameric H2M2-mediated catalysis of pyruvate or lactate are between those for the homotetrameric isozymes, M4 and H4, whereas the Vmax values are similar. The Km and Vmax values for H2M2-mediated catalysis of NADH are not significantly different among LDH isozymes. The values for activation energy and van't Hoff enthalpy changes for pyruvate reduction of H2M2 are between those for the homotetrameric isozymes. The temperature for half residual activity of H2M2 is closer to that for M4 than for H4 Sus scrofa
0.0026
-
(S)-lactate pH 8.5, 25°C, isozyme H4 Sus scrofa
0.0057
-
(S)-lactate pH 8.5, 25°C, isozyme H2M2 Sus scrofa
0.0127
-
NADH pH 8.5, 25°C, isozyme H2M2 Sus scrofa
0.0137
-
NADH pH 8.5, 25°C, isozyme H4 Sus scrofa
0.0142
-
(S)-lactate pH 8.5, 25°C, isozyme M4 Sus scrofa
0.0156
-
NADH pH 8.5, 25°C, isozyme M4 Sus scrofa
0.0468
-
pyruvate pH 8.5, 25°C, isozyme H4 Sus scrofa
0.0653
-
pyruvate pH 8.5, 25°C, isozyme H2M2 Sus scrofa
0.13
-
pyruvate pH 8.5, 25°C, isozyme M4 Sus scrofa

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Sus scrofa P00336 LDHB
-
Sus scrofa P00339 LDHA
-

Source Tissue

Source Tissue Comment Organism Textmining
brain contains a skeletal muscle type and heart type mixed heterotetrameric enzyme, H2M2 Sus scrofa
-
erythrocyte
-
Sus scrofa
-
eye
-
Sus scrofa
-
heart contains a heart type homotetrameric enzyme, H4 Sus scrofa
-
kidney
-
Sus scrofa
-
liver
-
Sus scrofa
-
lung
-
Sus scrofa
-
additional information in somatic cells, LDH forms homotetramers and heterotetramers that are encoded by two different genes: LDHA (skeletal muscle type, M) and LDHB (heart type, H) Sus scrofa
-
skeletal muscle contains a skeletal muscle type homotetrameric enzyme, M4 Sus scrofa
-
spleen
-
Sus scrofa
-
stomach
-
Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-lactate + NAD+
-
Sus scrofa pyruvate + NADH + H+
-
r
pyruvate + NADH + H+
-
Sus scrofa (S)-lactate + NAD+
-
r

Subunits

Subunits Comment Organism
heterotetramer the heterotetrameric LDH (H2M2) from swine brain is formed by two subunit of LDHA and two subunits of LDHB Sus scrofa
More in somatic cells, LDH forms homotetramers and heterotetramers that are encoded by two different genes: LDHA is the skeletal muscle type, M, isozyme, and LDHB is the heart type, H, isozyme Sus scrofa

Synonyms

Synonyms Comment Organism
lactate dehydrogenase
-
Sus scrofa
LDH
-
Sus scrofa
LdhA skeletal muscle type isozyme Sus scrofa
LDHB heart type isozyme Sus scrofa

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Sus scrofa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
assay at Sus scrofa

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Sus scrofa
NADH
-
Sus scrofa

General Information

General Information Comment Organism
metabolism lactate dehydrogenase (LDH) is a glycolytic enzyme that catalyzes the final step of glycolysis and produces NAD+ Sus scrofa