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Literature summary for 1.1.1.27 extracted from

  • Matoba, Y.; Miyasako, M.; Matsuo, K.; Oda, K.; Noda, M.; Higashikawa, F.; Kumagai, T.; Sugiyama, M.
    An alternative allosteric regulation mechanism of an acidophilic L-lactate dehydrogenase from Enterococcus mundtii 15-1A (2014), FEBS open bio, 4, 834-847.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.1.1.27

Activating Compound

Activating Compound Comment Organism Structure
D-fructose-1,6-bisphosphate enzyme binding structure, overview. The allosteric enzyme requires fructose-1,6-bisphosphate (FBP), an intermediate in the glycolysis pathway, for catalytic activities. FBP may play a role in stabilizing and maintaining the tetrameric structure Enterococcus mundtii
D-fructose-1,6-bisphosphate the allosteric enzyme requires fructose-1,6-bisphosphate (FBP), an intermediate in the glycolysis pathway, for catalytic activities. FBP may play a role in stabilizing and maintaining the tetrameric structure Enterococcus mundtii

Cloned(Commentary)

Cloned (Comment) Organism
gene ldh-1, DNA and amino acid sequence determinaation and analysis, sequence comparisons, recombinant expression in Escherichia coli Enterococcus mundtii
gene ldh-2, DNA and amino acid sequence determinaation and analysis, sequence comparisons, recombinant expression in Escherichia coli Enterococcus mundtii

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant wild-type enzyme, in apoform and in complex with fructose-1,6-bisphosphate and NADH, X-ray diffraction structure determination and analysis at 2.38 A and 2.30 A resolution, respectively, modelling Enterococcus mundtii

Protein Variants

Protein Variants Comment Organism
D241N site-directed mutagenesis, the mutant hsows higher activity at pH above 5.5 compared to the wild-type enzyme Enterococcus mundtii
E60Q site-directed mutagenesis, the mutant has a similar pH prodile as the wild-type Enterococcus mundtii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information alternative allosteric regulation mechanism of an acidophilic L-lactate dehydrogenase, kinetic analysis of the recombinant enzyme, overview Enterococcus mundtii
0.11
-
 NADH pH 7.5, temperature not specified in the publication, LDH-1, with 3 mM fructose-1,6-bisphosphate Enterococcus mundtii
0.18
-
 NADH pH 5.5, temperature not specified in the publication, LDH-1, with 3 mM fructose-1,6-bisphosphate Enterococcus mundtii
0.2
-
 NADH pH 5.5, temperature not specified in the publication, mutant D241N LDH-2, with 3 mM fructose-1,6-bisphosphate Enterococcus mundtii
0.26
-
 NADH pH 7.5, temperature not specified in the publication, mutant D241N LDH-2, with 3 mM fructose-1,6-bisphosphate Enterococcus mundtii
0.41
-
 NADH pH 5.5, temperature not specified in the publication, wild-type LDH-2, with 3 mM fructose-1,6-bisphosphate Enterococcus mundtii
0.9
-
 NADH pH 5.5, temperature not specified in the publication, mutant D241N LDH-2, without fructose-1,6-bisphosphate Enterococcus mundtii
0.93
-
 pyruvate pH 5.5, temperature not specified in the publication, LDH-1, with 3 mM fructose-1,6-bisphosphate Enterococcus mundtii
0.93
-
 NADH pH 7.5, temperature not specified in the publication, wild-type LDH-2, with 3 mM fructose-1,6-bisphosphate Enterococcus mundtii
2.2
-
 pyruvate pH 5.5, temperature not specified in the publication, wild-type LDH-2, with 3 mM fructose-1,6-bisphosphate Enterococcus mundtii
2.3
-
 pyruvate pH 5.5, temperature not specified in the publication, mutant D241N LDH-2, with 3 mM fructose-1,6-bisphosphate Enterococcus mundtii
2.7
-
 pyruvate pH 7.5, temperature not specified in the publication, wild-type LDH-2, with 3 mM fructose-1,6-bisphosphate Enterococcus mundtii
3
-
 pyruvate pH 7.5, temperature not specified in the publication, mutant D241N LDH-2, with 3 mM fructose-1,6-bisphosphate Enterococcus mundtii
3.8
-
 pyruvate pH 7.5, temperature not specified in the publication, LDH-1, with 3 mM fructose-1,6-bisphosphate Enterococcus mundtii
15
-
 pyruvate pH 5.5, temperature not specified in the publication, mutant D241N LDH-2, without fructose-1,6-bisphosphate Enterococcus mundtii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(S)-lactate + NAD+ Enterococcus mundtii
-
 pyruvate + NADH + H+
-
 r
(S)-lactate + NAD+ Enterococcus mundtii 15-1A
-
 pyruvate + NADH + H+
-
 r

Organism

Organism UniProt Comment Textmining
Enterococcus mundtii
-
 isolated from Brassica rapa L. subsp. nipposinica (L.H. Bailey) Hanelt var. linearifolia
-
Enterococcus mundtii A0A1A6GB48 LDH-1; isolated from Brassica rapa L. subsp. nipposinica (L.H. Bailey) Hanelt var. linearifolia
-
Enterococcus mundtii 15-1A
-
 isolated from Brassica rapa L. subsp. nipposinica (L.H. Bailey) Hanelt var. linearifolia
-
Enterococcus mundtii 15-1A A0A1A6GB48 LDH-1; isolated from Brassica rapa L. subsp. nipposinica (L.H. Bailey) Hanelt var. linearifolia
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-lactate + NAD+
-
 Enterococcus mundtii pyruvate + NADH + H+
-
 r
(S)-lactate + NAD+
-
 Enterococcus mundtii 15-1A pyruvate + NADH + H+
-
 r
additional information substrate binding structure, overview. The side chain of the Arg171 residue of LDH-2 seems to be important for the binding of pyruvate, pointing toward the pyruvate-binding site Enterococcus mundtii ?
-
 ?
additional information substrate binding structure, overview. The side chain of the Arg171 residue of LDH-2 seems to be important for the binding of pyruvate, pointing toward the pyruvate-binding site Enterococcus mundtii 15-1A ?
-
 ?

Subunits

Subunits Comment Organism
homotetramer each monomer has one active site, and the tetramer has two allosteric sites, each of which is situated at the Y-axis interface between two monomers Enterococcus mundtii
More secondary, tertiary, and quaternary structure analysis, and structure comparisons, overview.The subunit structure of L-LDH can be divided into N-terminal NADH-binding domain and C-terminal catalytic domain Enterococcus mundtii

Synonyms

Synonyms Comment Organism
L-LDH
-
 Enterococcus mundtii
LDH-1
-
 Enterococcus mundtii
LDH-2
-
 Enterococcus mundtii

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1300
-
 pyruvate pH 7.5, temperature not specified in the publication, wild-type LDH-2, with 3 mM fructose-1,6-bisphosphate Enterococcus mundtii
1500
-
 pyruvate pH 7.5, temperature not specified in the publication, LDH-1, with 3 mM fructose-1,6-bisphosphate Enterococcus mundtii
1600
-
 pyruvate pH 5.5, temperature not specified in the publication, LDH-1, with 3 mM fructose-1,6-bisphosphate Enterococcus mundtii
1800
-
 pyruvate pH 5.5, temperature not specified in the publication, wild-type and mutant D241N LDH-2, with 3 mM fructose-1,6-bisphosphate Enterococcus mundtii
1800
-
 pyruvate pH 7.5, temperature not specified in the publication, mutant D241N LDH-2, with 3 mM fructose-1,6-bisphosphate Enterococcus mundtii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
additional information
-
 detailed kinetic analysis of enzyme mutant D241N, done at pH 5.5 and pH 7.5 Enterococcus mundtii
5.5
-
-
 Enterococcus mundtii
5.5
-
 maximal activity at pH 5.5 which gradually decreases with the increase of pH Enterococcus mundtii

pH Range

pH Minimum pH Maximum Comment Organism
4 7.5 activity range, inactive at pH 8.0, profile overview Enterococcus mundtii
4 7.5 activity range, inactive at pH 8.0, profile overview. High level of activity between pH 4.0 and pH 7.5 Enterococcus mundtii

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Enterococcus mundtii
NADH
-
 Enterococcus mundtii
NADH enzyme binding structure, overview Enterococcus mundtii

General Information

General Information Comment Organism
evolution sequence identity between the Enterococcus mundtii LDH-1 and LDH-2 is 44.9% Enterococcus mundtii
physiological function alternative allosteric regulation mechanism of an acidophilic L-lactate dehydrogenase, overview. LDH-1 mainly plays a role in L-lactate production in Enterococcus mundtii, while LDH-2 plays another, different role Enterococcus mundtii

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
15
-
 pyruvate pH 7.5, temperature not specified in the publication, mutant D241N LDH-2, without fructose-1,6-bisphosphate Enterococcus mundtii
59
-
 pyruvate pH 5.5, temperature not specified in the publication, mutant D241N LDH-2, without fructose-1,6-bisphosphate Enterococcus mundtii
200
-
 NADH pH 7.5, temperature not specified in the publication, mutant D241N LDH-2, without fructose-1,6-bisphosphate Enterococcus mundtii
390
-
 pyruvate pH 7.5, temperature not specified in the publication, LDH-1, with 3 mM fructose-1,6-bisphosphate Enterococcus mundtii
480
-
 pyruvate pH 7.5, temperature not specified in the publication, wild-type LDH-2, with 3 mM fructose-1,6-bisphosphate Enterococcus mundtii
610
-
 pyruvate pH 7.5, temperature not specified in the publication, mutant D241N LDH-2, with 3 mM fructose-1,6-bisphosphate Enterococcus mundtii
790
-
 pyruvate pH 5.5, temperature not specified in the publication, mutant D241N LDH-2, with 3 mM fructose-1,6-bisphosphate Enterococcus mundtii
810
-
 pyruvate pH 5.5, temperature not specified in the publication, wild-type LDH-2, with 3 mM fructose-1,6-bisphosphate Enterococcus mundtii
1200
-
 NADH pH 5.5, temperature not specified in the publication, mutant D241N LDH-2, without fructose-1,6-bisphosphate Enterococcus mundtii
1400
-
 NADH pH 7.5, temperature not specified in the publication, wild-type LDH-2, with 3 mM fructose-1,6-bisphosphate Enterococcus mundtii
1700
-
 pyruvate pH 5.5, temperature not specified in the publication, LDH-1, with 3 mM fructose-1,6-bisphosphate Enterococcus mundtii
4400
-
 NADH pH 5.5, temperature not specified in the publication, wild-type LDH-2, with 3 mM fructose-1,6-bisphosphate Enterococcus mundtii
6800
-
 NADH pH 7.5, temperature not specified in the publication, mutant D241N LDH-2, with 3 mM fructose-1,6-bisphosphate Enterococcus mundtii
9000
-
 NADH pH 5.5, temperature not specified in the publication, LDH-1, with 3 mM fructose-1,6-bisphosphate Enterococcus mundtii
9000
-
 NADH pH 5.5, temperature not specified in the publication, mutant D241N LDH-2, with 3 mM fructose-1,6-bisphosphate Enterococcus mundtii
13000
-
 NADH pH 7.5, temperature not specified in the publication, LDH-1, with 3 mM fructose-1,6-bisphosphate Enterococcus mundtii