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Literature summary extracted from

  • Jackson, E.; Lopez-Gallego, F.; Guisan, J.; Betancor, L.
    Enhanced stability of L-lactate dehydrogenase through immobilization engineering (2016), Process Biochem., 51, 1248-1255.
No PubMed abstract available

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.27 additional information enhanced stability of L-lactate dehydrogenase through immobilization engineering, the enzyme is immobilized on glyoxyl-agarose, method optimization: preparation of an active and highly stable immobilizedderivative of LDH. with 90.1% immobilization and 72.0% yield is achieved using 300 mM trehalose during the immobilization process. Thermal stabilization factors attained for the immobilized LDH are 1600times greater as compared to its soluble counterpart. The immobilized preparation is also stabilized against ethanol where it recovers 75% of its initial activity after 48 h while the soluble enzyme is completely inactivated after only 10 min under the same conditions. Production of L-lactic acid is achieved in a batch reactor with the immobilized LDH and this preparation resists 15 reuses without the loss of activity. Co-immobilization of LDH and formate dehydrogenase. Immobilization has a negligible effect on the catalytic performance of L-LDH while having a significant impact on its stability Oryctolagus cuniculus

General Stability

EC Number General Stability Organism
1.1.1.27 PEG and trehalose stabilize the enzyme Oryctolagus cuniculus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.27 pyruvate substrate inhibition by pyruvate is related to the formation of an enzyme-pyruvate-NAD+complex Oryctolagus cuniculus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.27 additional information
-
 additional information Michaelis-Menten kinetics Oryctolagus cuniculus
1.1.1.27 0.13
-
 pyruvate soluble recombinant enzyme, pH 7.0, 25°C Oryctolagus cuniculus
1.1.1.27 0.133
-
 pyruvate immobilized recombinant enzyme, pH 7.0, 25°C Oryctolagus cuniculus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.27 140000
-
-
 Oryctolagus cuniculus

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+ Oryctolagus cuniculus
-
 pyruvate + NADH + H+
-
 r
1.1.1.27 additional information Oryctolagus cuniculus L-lactate dehydrogenase catalyzes the conversion of pyruvate to L-lactate using NADH as a cofactor ?
-
 ?
1.1.1.27 pyruvate + NADH + H+ Oryctolagus cuniculus
-
 (S)-lactate + NAD+
-
 r

Organic Solvent Stability

EC Number Organic Solvent Comment Organism
1.1.1.27 Ethanol the immobilized enzyme is also stabilized against ethanol where it recovers 75% of its initial activity after 48 h while the soluble enzyme is completely inactivated after only 10 min under the same conditions Oryctolagus cuniculus

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.27 Oryctolagus cuniculus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.1.1.27 skeletal muscle
-
 Oryctolagus cuniculus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.27 (S)-lactate + NAD+
-
 Oryctolagus cuniculus pyruvate + NADH + H+
-
 r
1.1.1.27 additional information L-lactate dehydrogenase catalyzes the conversion of pyruvate to L-lactate using NADH as a cofactor Oryctolagus cuniculus ?
-
 ?
1.1.1.27 pyruvate + NADH + H+
-
 Oryctolagus cuniculus (S)-lactate + NAD+
-
 r

Subunits

EC Number Subunits Comment Organism
1.1.1.27 homotetramer dimer of dimers, differential chemical crosstalk between the monomers Oryctolagus cuniculus

Synonyms

EC Number Synonyms Comment Organism
1.1.1.27 LDH
-
 Oryctolagus cuniculus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.27 45 55 recombinant enzyme, pyruvate reduction Oryctolagus cuniculus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.27 170.7
-
 pyruvate immobiized recombinant enzyme, pH 7.0, 25°C Oryctolagus cuniculus
1.1.1.27 276.5
-
 pyruvate soluble recombinant enzyme, pH 7.0, 25°C Oryctolagus cuniculus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.27 7
-
 recombinant enzyme, pyruvate reduction Oryctolagus cuniculus

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.27 NAD+
-
 Oryctolagus cuniculus
1.1.1.27 NADH
-
 Oryctolagus cuniculus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.1.1.27 3.29
-
 pyruvate immobiized recombinant enzyme, pH 7.0, 25°C Oryctolagus cuniculus
1.1.1.27 5.66
-
 pyruvate soluble recombinant enzyme, pH 7.0, 25°C Oryctolagus cuniculus