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Literature summary for 1.1.1.27 extracted from

  • Green, S.R.; Storey, K.B.
    Regulation of crayfish, Orconectes virilis, tail muscle lactate dehydrogenase (LDH) in response to anoxic conditions is associated with alterations in phosphorylation patterns (2016), Comp. Biochem. Physiol. B, 202, 67-74.
    View publication on PubMed
Search for more literature for 1.1.1.27

Inhibitors

Inhibitors Comment Organism Structure
pyruvate low substrate inhibition Faxonius virilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Vmax in the pyruvate-reducing direction is significantly higher for the enzyme from anoxic crayfish whereas in the lactate-oxidizing direction the Vmax is significantly higher for the aerobic control enzyme Faxonius virilis
0.123
-
 pyruvate aerobic control enzyme, pH 6.7, 25°C Faxonius virilis
0.19
-
 pyruvate anoxic enzyme, pH 6.7, 25°C Faxonius virilis
0.353
-
 pyruvate anoxic enzyme, pH 7.2, 25°C Faxonius virilis
0.36
-
 pyruvate aerobic control enzyme, pH 7.2, 25°C Faxonius virilis
1.96
-
 NAD+ anoxic enzyme, pH 8.5, 25°C Faxonius virilis
2.18
-
 NAD+ aerobic control enzyme, pH 8.5, 25°C Faxonius virilis
22
-
 (S)-lactate anoxic enzyme, pH 6.7, 25°C Faxonius virilis
32.9
-
 (S)-lactate aerobic control enzyme, pH 8.5, 25°C Faxonius virilis
34.2
-
 (S)-lactate anoxic enzyme, pH 8.5, 25°C Faxonius virilis

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Faxonius virilis
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein purified LDH from aerobic control crayfish shows significantly higher amounts of serine/threonine phosphorylation than does the anoxic enzyme form Faxonius virilis

Purification (Commentary)

Purification (Comment) Organism
native enzyme to homogeneity from tail muscle of both aerobic control and anoxic crayfish 26.5fold and 69.4fold, respectively, by anion exchange chromatography and two steps of affinity chromatography Faxonius virilis

Source Tissue

Source Tissue Comment Organism Textmining
tail muscle
-
 Faxonius virilis
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
7.35
-
 purified native aerobic control enzyme, pH 7.2, 25°C, pyruvate reduction Faxonius virilis
15.8
-
 purified native anoxic enzyme, pH 7.2, 25°C, pyruvate reduction Faxonius virilis

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
lactate dehydrogenase
-
 Faxonius virilis
LDH
-
 Faxonius virilis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Faxonius virilis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
 the enzyme from aerobic control muscle has a significantly higher melting temperature (greater thermal stability) compared to the anoxic enzyme form, suggesting that there is a structural difference between the two enzyme forms. Both anoxic and control LDH are most thermally stable around pH 7.6 although the difference in TM between pH 7.3 and pH 7.6 is not significant for the anoxic LDH Faxonius virilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
 assay at, pyruvate reduction Faxonius virilis
8.5
-
 assay at, (S)-lactate oxidation Faxonius virilis

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Faxonius virilis
NADH
-
 Faxonius virilis

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
20.4
-
 anoxic enzyme, pH 7.2, 25°C Faxonius virilis pyruvate
30.3
-
 aerobic control enzyme, pH 7.2, 25°C Faxonius virilis pyruvate

General Information

General Information Comment Organism
physiological function lactate dehydrogenase is the terminal enzyme of anaerobic glycolysis, and has a crucial role in sustaining ATP production by glycolysis during periods of anoxia via regenerating NAD+ through the production of lactate. Anoxia-induced modifications of crayfish muscle LDH may contribute significantly to modulating enzyme function under anoxic conditions Faxonius virilis