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Literature summary extracted from

  • Jiang, T.; Xu, Y.; Sun, X.; Zheng, Z.; Ouyang, J.
    Kinetic characterization of recombinant Bacillus coagulans FDP-activated L-lactate dehydrogenase expressed in Escherichia coli and its substrate specificity (2014), Protein Expr. Purif., 95, 219-225.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.1.1.27 D-fructose-1,6-bisphosphate best at 4-9 mM Weizmannia coagulans
1.1.1.27 additional information the enzyme also shows some activity in the absence of D-fructose-1,6-bisphosphate, with a pH optimum of pH 4.0 Weizmannia coagulans

Application

EC Number Application Comment Organism
1.1.1.27 synthesis L-nLDH is an efficient catalyst that can be used in the enantioselective reduction of alpha-keto acids to alpha-hydroxy acids Weizmannia coagulans

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.27 gene ldhL, DNA and amino acid sequence determination and analysis, recombinant expression of His6-tagged enzyme in Escherichia coli BL21(DE3) Weizmannia coagulans

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.27 Co2+
-
 Weizmannia coagulans
1.1.1.27 Cu2+
-
 Weizmannia coagulans
1.1.1.27 Ni2+ strong inhibition Weizmannia coagulans
1.1.1.27 Zn2+
-
 Weizmannia coagulans

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.27 1.91
-
 pyruvate recombinant enzyme, pH 6.5, 55°C Weizmannia coagulans

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.1.27 cytoplasm
-
 Weizmannia coagulans 5737
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.27 Ba2+ activates Weizmannia coagulans
1.1.1.27 Ca2+ activates, most effective divalent metal ion Weizmannia coagulans
1.1.1.27 Mg2+ activates Weizmannia coagulans
1.1.1.27 Mn2+ activates Weizmannia coagulans
1.1.1.27 additional information Ca2+, Ba2+, and Mg2+ ions are as effective as Mn2+ at pH 6.5 in enzyme activation Weizmannia coagulans

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+ Weizmannia coagulans
-
 pyruvate + NADH + H+
-
 r
1.1.1.27 (S)-lactate + NAD+ Weizmannia coagulans NL01
-
 pyruvate + NADH + H+
-
 r
1.1.1.27 pyruvate + NADH + H+ Weizmannia coagulans
-
 (S)-lactate + NAD+
-
 r
1.1.1.27 pyruvate + NADH + H+ Weizmannia coagulans NL01
-
 (S)-lactate + NAD+
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.27 Weizmannia coagulans W8CXQ9
-
-
1.1.1.27 Weizmannia coagulans NL01 W8CXQ9
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.27 recombinant His6-tagged enzyme from Escherichia coli BL21(DE3) by metal affinity chromatography dialysis, and ultrafiltration Weizmannia coagulans

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.1.27 351
-
 purified recombinant enzyme, pH 11.5, 55°C, lactate oxidation Weizmannia coagulans
1.1.1.27 2323
-
 purified recombinant enzyme, pH 6.5, 55°C, pyruvate reduction Weizmannia coagulans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.27 (S)-lactate + NAD+
-
 Weizmannia coagulans pyruvate + NADH + H+
-
 r
1.1.1.27 (S)-lactate + NAD+
-
 Weizmannia coagulans NL01 pyruvate + NADH + H+
-
 r
1.1.1.27 2-oxobutyrate + NADH + H+ low activity Weizmannia coagulans 2-hydroxybutyrate + NAD+
-
 ?
1.1.1.27 2-oxobutyrate + NADH + H+ low activity Weizmannia coagulans NL01 2-hydroxybutyrate + NAD+
-
 ?
1.1.1.27 ethyl pyruvate + NADH + H+
-
 Weizmannia coagulans ? + NAD+
-
 ?
1.1.1.27 ethyl pyruvate + NADH + H+
-
 Weizmannia coagulans NL01 ? + NAD+
-
 ?
1.1.1.27 methyl pyruvate + NADH + H+
-
 Weizmannia coagulans ? + NAD+
-
 ?
1.1.1.27 additional information L-nLDH shows higher specificity towards pyruvate esters, such as methyl pyruvate and ethyl pyruvate. Very poor activity with 4-methyl-2-oxovalerate Weizmannia coagulans ?
-
 ?
1.1.1.27 additional information L-nLDH shows higher specificity towards pyruvate esters, such as methyl pyruvate and ethyl pyruvate. Very poor activity with 4-methyl-2-oxovalerate Weizmannia coagulans NL01 ?
-
 ?
1.1.1.27 phenylpyruvate + NADH + H+ low activity Weizmannia coagulans L-phenyllactate + NAD+
-
 ?
1.1.1.27 pyruvate + NADH + H+
-
 Weizmannia coagulans (S)-lactate + NAD+
-
 r
1.1.1.27 pyruvate + NADH + H+
-
 Weizmannia coagulans NL01 (S)-lactate + NAD+
-
 r

Subunits

EC Number Subunits Comment Organism
1.1.1.27 ? x * 34000-36000, recombinant enzyme, SDS-PAGE Weizmannia coagulans

Synonyms

EC Number Synonyms Comment Organism
1.1.1.27 L-nLDH
-
 Weizmannia coagulans
1.1.1.27 ldhL
-
 Weizmannia coagulans

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.27 55
-
 recombinant enzyme, pyruvate reduction and lactate oxidation Weizmannia coagulans

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.1.1.27 50
-
 purified recombinant enzyme, half-time for inactivation is about 4 h and no residual activity is determined after 9 h, rapid loss of activity above Weizmannia coagulans

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.27 additional information
-
 the enzyme also shows some activity in the absence of D-fructose-1,6-bisphosphate (FDP), with a pH optimum of pH 4.0. The addition of FDP results in a shift of pH optimum in pyruvate reduction, overview Weizmannia coagulans
1.1.1.27 6.5
-
 recombinant enzyme, pyruvate reduction Weizmannia coagulans
1.1.1.27 11.5
-
 recombinant enzyme, lactate oxidation Weizmannia coagulans

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.1.1.27 4.5 9.5 activity range, inactive at pH 4.0 and pH 10.0 Weizmannia coagulans

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.27 NAD+
-
 Weizmannia coagulans
1.1.1.27 NADH
-
 Weizmannia coagulans

General Information

EC Number General Information Comment Organism
1.1.1.27 evolution there are two types of L-nLDHs, non-allosteric L-nLDHs and allosteric L-nLDHs Weizmannia coagulans
1.1.1.27 metabolism NAD-dependent L-lactate dehydrogenases (L-nLDHs) catalyze the last step of anaerobic glycosis, the reduction of pyruvate to L-lactate, concomitantly oxidizing NADH into NAD+ Weizmannia coagulans
1.1.1.27 additional information the key catalytic residues Arg109, Asp168, Arg171, and His 195, are conserved in Bacillus coagulans strain NL01 L-nLDH Weizmannia coagulans
1.1.1.27 physiological function the stereospecific L-LDH is a fructose 1,6-diphosphate-activated NAD-dependent lactate dehydrogenase, L-nLDH Weizmannia coagulans