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Literature summary extracted from

  • Terlecki, G.; Czapi?ska, E.; Hotowy, K.
    Ultracentrifugation studies of the location of the site involved in the interaction of pig heart lactate dehydrogenase with acidic phospholipids at low pH. A comparison with the muscle form of the enzyme (2007), Cell. Mol. Biol. Lett., 12, 378-395.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.27 additional information NADH, NAD+, ATP, ADP, AMP, and pyruvate inhibit the interaction of the heart-type isozyme with acidic phospholipid liposomes, potency in descending order. NADP+, GTP, CTP, UTP and lactate are ineffective, overview Sus scrofa

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.27 Sus scrofa
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.1.1.27 commercial preparation
-
 Sus scrofa
-
1.1.1.27 heart heart-type isozyme Sus scrofa
-
1.1.1.27 skeletal muscle muscle-type isozyme, i.e. M4 isoform Sus scrofa
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.27 (S)-lactate + NAD+
-
 Sus scrofa pyruvate + NADH + H+
-
 r
1.1.1.27 additional information the heart-type isozyme interacts with liposomes made of acidic phospholipids, such as phosphatidylserine or cardiolipin, most effectively at low pH close to the isoelectric point of the isozyme of pH 5.5 strongly involving the enzyme's NADH-cofactor binding site, no interaction with liposomes of the muscle-type isozyme, overview Sus scrofa ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.1.27 tetramer heart-type isozyme Sus scrofa

Synonyms

EC Number Synonyms Comment Organism
1.1.1.27 heart LDH
-
 Sus scrofa
1.1.1.27 lactate dehydrogenase
-
 Sus scrofa
1.1.1.27 LDH
-
 Sus scrofa
1.1.1.27 muscle LDH
-
 Sus scrofa

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.27 25
-
 assay at Sus scrofa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.27 7.5
-
 assay at Sus scrofa

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.27 NAD+
-
 Sus scrofa
1.1.1.27 NADH the NADH-cofactor binding site of heart LDH is involved in the interaction of the isozyme with liposomes made of acidic phospholipids, overview Sus scrofa

pI Value

EC Number Organism Comment pI Value Maximum pI Value
1.1.1.27 Sus scrofa heart-type isozyme
-
 5.5