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Literature summary for 1.1.1.27 extracted from

  • Waldvogel, S.; Weber, H.; Zuber, H.
    Structure and function of L-lactate dehydrogenase from thermophilic and mesophilic bacteria VII (1987), Biol. Chem. Hoppe-Seyler, 368, 1391-1399.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
D-fructose 1,6-bisphosphate activates wild-type enzyme Geobacillus stearothermophilus
D-fructose 1,6-bisphosphate activates wild-type enzyme Priestia megaterium

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli HB101 using a pEMBL vector. The gene is strongly expressed in the vector used if the orientation of the insert allows the LDH promoter and the vector's lac promoter to direct transcription in the same direction Geobacillus stearothermophilus
expression in Escherichia coli HB101 using a pEMBL vector. The gene is strongly expressed in the vector used if the orientation of the insert allows the LDH promoter and the vector's lac promoter to direct transcription in the same direction Priestia megaterium

Protein Variants

Protein Variants Comment Organism
S100M a hybrid gene is constructed from fragments of the LDH genes from Bacillus stearothermophilus (coding for aa 15-100) and Bacillus megaterium (coding for aa 101-331). The hybrid LDH, named S100M, is more thermostable than Bacillus megaterium LDH, less thermostable than Bacillus stearothermophilus LDH and unlike the two wild-type enzymes, it can not be activated by D-fructose 1,6-bisphosphate Geobacillus stearothermophilus
S100M a hybrid gene is constructed from fragments of the LDH genes from Bacillus stearothermophilus (coding for aa 15-100) and Bacillus megaterium (coding for aa 101-331). The hybrid LDH, named S100M, is more thermostable than Bacillus megaterium LDH, less thermostable than Bacillus stearothermophilus LDH and unlike the two wild-type enzymes, it can not be activated by D-fructose 1,6-bisphosphate Priestia megaterium

Inhibitors

Inhibitors Comment Organism Structure
D-fructose 1,6-bisphosphate slightly inhibits activity of hybrid enzyme constructed from fragments of the LDH genes from Bacillus stearothermophilus (coding for aa 15-100) and Bacillus megaterium (coding for aa 101-331) Geobacillus stearothermophilus
D-fructose 1,6-bisphosphate slightly inhibits activity of hybrid enzyme constructed from fragments of the LDH genes from Bacillus stearothermophilus (coding for aa 15-100) and Bacillus megaterium (coding for aa 101-331) Priestia megaterium

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.05
-
NADH measured without D-fructose 1,6-bisphosphate, wild-type enzyme Geobacillus stearothermophilus
0.08
-
NADH measured with D-fructose 1,6-bisphosphate, wild-type enzyme Geobacillus stearothermophilus
0.15
-
NADH measured without D-fructose 1,6-bisphosphate, wild-type enzyme Priestia megaterium
0.18
-
NADH measured with D-fructose 1,6-bisphosphate, wild-type enzyme Priestia megaterium
0.19
-
NADH measured with D-fructose 1,6-bisphosphate Geobacillus stearothermophilus
0.19
-
NADH measured with D-fructose 1,6-bisphosphate Priestia megaterium
0.19
-
NADH measured without D-fructose 1,6-bisphosphate, hybrid enzyme constructed from fragments of the LDH genes from Bacillus stearothermophilus (coding for aa 15-100) and Bacillus megaterium (coding for aa 101-331) Geobacillus stearothermophilus
0.19
-
NADH measured without D-fructose 1,6-bisphosphate, hybrid enzyme constructed from fragments of the LDH genes from Bacillus stearothermophilus (coding for aa 15-100) and Bacillus megaterium (coding for aa 101-331) Priestia megaterium
0.2
-
pyruvate measured with D-fructose 1,6-bisphosphate, wild-type enzyme Geobacillus stearothermophilus
0.8
-
pyruvate measured with D-fructose 1,6-bisphosphate, wild-type enzyme Priestia megaterium
6.8
-
pyruvate measured with D-fructose 1,6-bisphosphate, hybrid enzyme constructed from fragments of the LDH genes from Bacillus stearothermophilus (coding for aa 15-100) and Bacillus megaterium (coding for aa 101-331) Geobacillus stearothermophilus
6.8
-
pyruvate measured with D-fructose 1,6-bisphosphate, hybrid enzyme constructed from fragments of the LDH genes from Bacillus stearothermophilus (coding for aa 15-100) and Bacillus megaterium (coding for aa 101-331) Priestia megaterium
7
-
pyruvate measured without D-fructose 1,6-bisphosphate, hybrid enzyme constructed from fragments of the LDH genes from Bacillus stearothermophilus (coding for aa 15-100) and Bacillus megaterium (coding for aa 101-331) Geobacillus stearothermophilus
7
-
pyruvate measured without D-fructose 1,6-bisphosphate, hybrid enzyme constructed from fragments of the LDH genes from Bacillus stearothermophilus (coding for aa 15-100) and Bacillus megaterium (coding for aa 101-331) Priestia megaterium
13
-
pyruvate measured without D-fructose 1,6-bisphosphate, wild-type enzyme Geobacillus stearothermophilus
34
-
pyruvate measured without D-fructose 1,6-bisphosphate, wild-type enzyme Priestia megaterium

Organism

Organism UniProt Comment Textmining
Geobacillus stearothermophilus
-
-
-
Priestia megaterium
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pyruvate + NADH + H+
-
Geobacillus stearothermophilus (S)-lactate + NAD+
-
?
pyruvate + NADH + H+
-
Priestia megaterium (S)-lactate + NAD+
-
?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
a hybrid gene is constructed from fragments of the LDH genes from Bacillus stearothermophilus (coding for aa 15-100) and Bacillus megaterium (coding for aa 101-331). The hybrid LDH, named S100M, is more thermostable than Bacillus megaterium LDH, less thermostable than Bacillus stearothermophilus LDH and unlike the two wild-type enzymes, it can not be activated by D-fructose 1,6-bisphosphate Geobacillus stearothermophilus
additional information
-
a hybrid gene is constructed from fragments of the LDH genes from Bacillus stearothermophilus (coding for aa 15-100) and Bacillus megaterium (coding for aa 101-331). The hybrid LDH, named S100M, is more thermostable than Bacillus megaterium LDH, less thermostable than Bacillus stearothermophilus LDH and unlike the two wild-type enzymes, it can not be activated by D-fructose 1,6-bisphosphate Priestia megaterium
48
-
30 min, stable up to Priestia megaterium
58
-
30 min, stable up to A hybrid gene is constructed from fragments of the LDH genes from Bacillus stearothermophilus (coding for aa 15-100) and Bacillus megaterium (coding for aa 101-331). The hybrid LDH is named S100M Geobacillus stearothermophilus
58
-
30 min, stable up to A hybrid gene is constructed from fragments of the LDH genes from Bacillus stearothermophilus (coding for aa 15-100) and Bacillus megaterium (coding for aa 101-331). The hybrid LDH is named S100M Priestia megaterium
74
-
30 min, stable up to Geobacillus stearothermophilus