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Literature summary for 1.1.1.27 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
Search for more literature for 1.1.1.27

Protein Variants

Protein Variants Comment Organism
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

General Stability Organism
PEG and trehalose stabilize the enzyme Oryctolagus cuniculus

Inhibitors

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

KM Value [mM]

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

Organic Solvent Stability

Organic Solvent Comment Organism
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

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
skeletal muscle
-
 Oryctolagus cuniculus
-

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms Comment Organism
LDH
-
 Oryctolagus cuniculus

Temperature Optimum [°C]

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

Turnover Number [1/s]

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Oryctolagus cuniculus
NADH
-
 Oryctolagus cuniculus

Ki Value [mM]

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