BRENDA - Enzyme Database show
show all sequences of 1.1.1.28

Diverse allosteric and catalytic functions of tetrameric D-lactate dehydrogenases from three Gram-negative bacteria

Furukawa, N.; Miyanaga, A.; Togawa, M.; Nakajima, M.; Taguchi, H.; AMB Express 4, 76 (2014)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
fructose 1,6-bisphosphate
required
Fusobacterium nucleatum subsp. nucleatum
fructose 1,6-bisphosphate
required
Pseudomonas aeruginosa
additional information
no activation of the enzyme by fructose 1,6-bisphosphate and Mg2+
Escherichia coli
Cloned(Commentary)
Commentary
Organism
gene ecd_01352, recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta2 (DE3)
Escherichia coli
gene fn0511, recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta2 (DE3)
Fusobacterium nucleatum subsp. nucleatum
gene pa0927, recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta2 (DE3)
Pseudomonas aeruginosa
Inhibitors
Inhibitors
Commentary
Organism
Structure
glyoxylate
-
Pseudomonas aeruginosa
Hydroxypyruvate
-
Pseudomonas aeruginosa
oxaloacetate
-
Escherichia coli
oxaloacetate
-
Fusobacterium nucleatum subsp. nucleatum
oxamate
constant inhibition at pH 7.0 and pH 8.0
Escherichia coli
oxamate
inhibits the catalytic reaction of FNLDH competitively with pyruvate, but markedly enhances the enzyme reaction at low concentration through canceling of the apparent homotropic cooperativity at pH 8.0
Fusobacterium nucleatum subsp. nucleatum
oxamate
inhibits the catalytic reaction of PALDH in a mixed--type manner at pH 7.0, but markedly enhances the enzyme reaction at low concentration through canceling of the apparent homotropic cooperativity at pH 8.0
Pseudomonas aeruginosa
phenylpyruvate
-
Fusobacterium nucleatum subsp. nucleatum
pyruvate
-
Pseudomonas aeruginosa
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetics and allosteric mechanism of D-LDHs, overview. The enzyme shows a hyperbolic shaped pyruvate saturation curve below pH 6.5, and shows positive cooperativity in the pyruvate saturation curve above pH 7.5
Escherichia coli
additional information
-
additional information
kinetics and allosteric mechanism of D-LDHs, overview. The enzyme shows a hyperbolic shaped pyruvate saturation curve below pH 6.5, and shows positive cooperativity in the pyruvate saturation curve above pH 7.5
Fusobacterium nucleatum subsp. nucleatum
additional information
-
additional information
kinetics and allosteric mechanism of D-LDHs, overview. The enzyme shows a hyperbolic shaped pyruvate saturation curve below pH 6.5, and shows negative cooperativity in the pyruvate saturation curve above pH 7.5
Pseudomonas aeruginosa
0.019
-
NADH
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
0.022
-
NADH
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
0.028
-
NADH
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
Fusobacterium nucleatum subsp. nucleatum
0.031
-
NADH
pH 8.0, 30°C, recombinant enzyme, with Mg2+
Fusobacterium nucleatum subsp. nucleatum
0.035
-
NADH
pH 8.0, 30°C, recombinant enzyme, with or without fructose 1,6-bisphosphate and Mg2+
Pseudomonas aeruginosa
0.036
-
NADH
pH 8.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
0.055
-
NADH
pH 7.0, 30°C, recombinant enzyme
Escherichia coli
0.088
-
NADH
pH 8.0, 30°C, recombinant enzyme
Escherichia coli
0.09
-
NADH
pH 8.0, 30°C, recombinant enzyme, with Mg2+
Escherichia coli
0.092
-
NADH
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
Escherichia coli
0.1
-
pyruvate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
0.31
-
2-oxobutyrate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
0.34
-
pyruvate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
0.36
-
pyruvate
pH 8.0, 30°C, recombinant enzyme, with Mg2+
Pseudomonas aeruginosa
0.64
-
2-oxobutyrate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
0.68
-
2-oxovalerate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
0.85
-
pyruvate
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
Pseudomonas aeruginosa
1.2
-
pyruvate
pH 8.0, 30°C, recombinant enzyme, with Mg2+
Fusobacterium nucleatum subsp. nucleatum
1.2
-
pyruvate
pH 8.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
1.7
-
oxaloacetate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
1.7
-
pyruvate
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
Fusobacterium nucleatum subsp. nucleatum
2.5
-
oxaloacetate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
2.5
-
pyruvate
pH 8.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
2.6
-
2-oxocaproate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
2.6
-
pyruvate
pH 7.0, 30°C, recombinant enzyme
Escherichia coli
3
-
Hydroxypyruvate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
3.5
-
2-oxoisovalerate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
3.8
-
2-oxoisocaproate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
4
-
2-oxovalerate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
5.8
-
2-oxocaproate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
6.5
-
pyruvate
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
Escherichia coli
6.8
-
glyoxylate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
7.1
-
phenylpyruvate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
7.2
-
pyruvate
pH 8.0, 30°C, recombinant enzyme, with Mg2+
Escherichia coli
7.6
-
pyruvate
pH 8.0, 30°C, recombinant enzyme
Escherichia coli
11
-
phenylpyruvate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
12
-
2-oxoisocaproate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
12
-
Hydroxypyruvate
pH 7.0, 30°C, recombinant enzyme
Escherichia coli
18
-
glyoxylate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
18
-
Hydroxypyruvate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
20
-
glyoxylate
pH 7.0, 30°C, recombinant enzyme
Escherichia coli
30
-
2-oxobutyrate
pH 7.0, 30°C, recombinant enzyme
Escherichia coli
54
-
oxaloacetate
pH 7.0, 30°C, recombinant enzyme
Escherichia coli
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
activates
Fusobacterium nucleatum subsp. nucleatum
Mg2+
activates
Pseudomonas aeruginosa
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
37800
-
-
Pseudomonas aeruginosa
38500
-
-
Escherichia coli
40000
-
4 * 40000, about, sequence calculation
Fusobacterium nucleatum subsp. nucleatum
120000
-
recombinant His-tagged enzyme, gel filtration
Pseudomonas aeruginosa
150000
-
recombinant His-tagged enzyme, peak 2, gel filtration
Escherichia coli
160000
-
recombinant His-tagged enzyme, gel filtration
Fusobacterium nucleatum subsp. nucleatum
330000
-
recombinant His-tagged enzyme, peak 1, gel filtration
Escherichia coli
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(R)-lactate + NAD+
Fusobacterium nucleatum subsp. nucleatum
-
pyruvate + NADH + H+
-
-
r
(R)-lactate + NAD+
Escherichia coli
-
pyruvate + NADH + H+
-
-
r
pyruvate + NADH + H+
Pseudomonas aeruginosa
-
(R)-lactate + NAD+
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
A0A140N893
-
-
Fusobacterium nucleatum subsp. nucleatum
Q8RG11
strain JCM 8532
-
Fusobacterium nucleatum subsp. nucleatum ATCC 25586 / JCM14847
Q8RG11
strain JCM 8532
-
Pseudomonas aeruginosa
Q9I530
-
-
Purification (Commentary)
Commentary
Organism
recombinant His-tagged enzyme from Escherichia coli strain Rosetta2 (DE3) by two different steps of affinity chromatography, and ultrafiltration
Escherichia coli
recombinant His-tagged enzyme from Escherichia coli strain Rosetta2 (DE3) by two different steps of affinity chromatography, and ultrafiltration
Fusobacterium nucleatum subsp. nucleatum
recombinant His-tagged enzyme from Escherichia coli strain Rosetta2 (DE3) by two different steps of affinity chromatography, and ultrafiltration
Pseudomonas aeruginosa
Reaction
Reaction
Commentary
Organism
(R)-lactate + NAD+ = pyruvate + NADH + H+
allosteric mechanism
Escherichia coli
(R)-lactate + NAD+ = pyruvate + NADH + H+
allosteric mechanism
Fusobacterium nucleatum subsp. nucleatum
(R)-lactate + NAD+ = pyruvate + NADH + H+
allosteric mechanism
Pseudomonas aeruginosa
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(R)-lactate + NAD+
-
739841
Fusobacterium nucleatum subsp. nucleatum
pyruvate + NADH + H+
-
-
-
r
(R)-lactate + NAD+
-
739841
Escherichia coli
pyruvate + NADH + H+
-
-
-
r
2-oxobutyrate + NADH + H+
-
739841
Fusobacterium nucleatum subsp. nucleatum
2-hydroxybutyrate + NAD+
-
-
-
r
2-oxobutyrate + NADH + H+
-
739841
Pseudomonas aeruginosa
2-hydroxybutyrate + NAD+
-
-
-
r
2-oxobutyrate + NADH + H+
-
739841
Escherichia coli
2-hydroxybutyrate + NAD+
-
-
-
r
2-oxobutyrate + NADH + H+
-
739841
Fusobacterium nucleatum subsp. nucleatum ATCC 25586 / JCM14847
2-hydroxybutyrate + NAD+
-
-
-
r
2-oxocaproate + NADH + H+
-
739841
Fusobacterium nucleatum subsp. nucleatum
2-hydroxycaproate + NAD+
-
-
-
r
2-oxocaproate + NADH + H+
-
739841
Pseudomonas aeruginosa
2-hydroxycaproate + NAD+
-
-
-
r
2-oxocaproate + NADH + H+
-
739841
Fusobacterium nucleatum subsp. nucleatum ATCC 25586 / JCM14847
2-hydroxycaproate + NAD+
-
-
-
r
2-oxoisocaproate + NADH + H+
-
739841
Fusobacterium nucleatum subsp. nucleatum
2-hydroxyisocaproate + NAD+
-
-
-
r
2-oxoisocaproate + NADH + H+
-
739841
Pseudomonas aeruginosa
2-hydroxyisocaproate + NAD+
-
-
-
r
2-oxoisovalerate + NADH + H+
-
739841
Fusobacterium nucleatum subsp. nucleatum
2-hydroxyisovalerate + NAD+
-
-
-
r
2-oxovalerate + NADH + H+
-
739841
Fusobacterium nucleatum subsp. nucleatum
2-hydroxyvalerate + NAD+
-
-
-
r
2-oxovalerate + NADH + H+
-
739841
Pseudomonas aeruginosa
2-hydroxyvalerate + NAD+
-
-
-
r
glyoxylate + NADH + H+
-
739841
Fusobacterium nucleatum subsp. nucleatum
hydroxyacetate + NAD+
-
-
-
r
glyoxylate + NADH + H+
-
739841
Pseudomonas aeruginosa
hydroxyacetate + NAD+
-
-
-
r
glyoxylate + NADH + H+
-
739841
Escherichia coli
hydroxyacetate + NAD+
-
-
-
r
hydroxypyruvate + NADH + H+
-
739841
Fusobacterium nucleatum subsp. nucleatum
glycerate + NAD+
-
-
-
r
hydroxypyruvate + NADH + H+
-
739841
Pseudomonas aeruginosa
glycerate + NAD+
-
-
-
r
hydroxypyruvate + NADH + H+
-
739841
Escherichia coli
glycerate + NAD+
-
-
-
r
hydroxypyruvate + NADH + H+
-
739841
Fusobacterium nucleatum subsp. nucleatum ATCC 25586 / JCM14847
glycerate + NAD+
-
-
-
r
additional information
the enzyme ECLDH exhibits high substrate specificity toward pyruvate. No or poor activity with 2-oxovalerate, 2-oxoisovalerate, 2-oxocaproate, 2-oxoisocaproate, phenylpyruvate, and hydroxyphenylpyruvate
739841
Escherichia coli
?
-
-
-
-
additional information
the enzyme FNLDH exhibits a broad substrate specificity toward hydrophobic 2-oxoacids such as 2-oxobutyrate and 2-oxovalerate. Poor activity with hydroxyphenylpyruvate and 2-oxoisovalerate
739841
Fusobacterium nucleatum subsp. nucleatum
?
-
-
-
-
additional information
the enzyme PALDH exhibits high substrate specificity toward pyruvate. Poor activity with hydroxyphenylpyruvate and 2-oxoisovalerate
739841
Pseudomonas aeruginosa
?
-
-
-
-
additional information
the enzyme FNLDH exhibits a broad substrate specificity toward hydrophobic 2-oxoacids such as 2-oxobutyrate and 2-oxovalerate. Poor activity with hydroxyphenylpyruvate and 2-oxoisovalerate
739841
Fusobacterium nucleatum subsp. nucleatum ATCC 25586 / JCM14847
?
-
-
-
-
oxaloacetate + NADH + H+
-
739841
Fusobacterium nucleatum subsp. nucleatum
malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
-
739841
Pseudomonas aeruginosa
malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
-
739841
Escherichia coli
malate + NAD+
-
-
-
r
phenylpyruvate + NADH + H+
-
739841
Fusobacterium nucleatum subsp. nucleatum
D-phenyllactate + NAD+
-
-
-
r
phenylpyruvate + NADH + H+
-
739841
Pseudomonas aeruginosa
D-phenyllactate + NAD+
-
-
-
r
pyruvate + NADH + H+
-
739841
Fusobacterium nucleatum subsp. nucleatum
(R)-lactate + NAD+
-
-
-
r
pyruvate + NADH + H+
-
739841
Pseudomonas aeruginosa
(R)-lactate + NAD+
-
-
-
r
pyruvate + NADH + H+
-
739841
Escherichia coli
(R)-lactate + NAD+
-
-
-
r
pyruvate + NADH + H+
-
739841
Fusobacterium nucleatum subsp. nucleatum ATCC 25586 / JCM14847
(R)-lactate + NAD+
-
-
-
r
Subunits
Subunits
Commentary
Organism
homooctamer
8 * 38500, about, sequence calculation, the apparently octameric form of ECLDH is likely an artificial product due to the overexpression, and exhibits slightly but significantly lower specific activity than the tetrameric form
Escherichia coli
homotetramer
4 * 38500, about, sequence calculation
Escherichia coli
homotetramer
4 * 40000, about, sequence calculation
Fusobacterium nucleatum subsp. nucleatum
homotrimer
4 * 37800, about, sequence calculation
Pseudomonas aeruginosa
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Escherichia coli
30
-
assay at
Fusobacterium nucleatum subsp. nucleatum
30
-
assay at
Pseudomonas aeruginosa
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
39
-
purified recombinant His-tagged enzyme, pH 8.0, stable up to
Fusobacterium nucleatum subsp. nucleatum
49
-
purified recombinant His-tagged enzyme, pH 8.0, stable up to
Escherichia coli
57
-
purified recombinant His-tagged enzyme, pH 5.0, stable up to
Pseudomonas aeruginosa
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
11
-
glyoxylate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
18
-
phenylpyruvate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
31
-
2-oxobutyrate
pH 7.0, 30°C, recombinant enzyme
Escherichia coli
39
-
2-oxoisocaproate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
50
-
Hydroxypyruvate
pH 7.0, 30°C, recombinant enzyme
Escherichia coli
69
-
2-oxovalerate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
80
-
NADH
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
Fusobacterium nucleatum subsp. nucleatum
80
-
oxaloacetate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
80
-
pyruvate
pH 7.0, 30°C, recombinant enzyme; pH 8.0, 30°C, recombinant enzyme, with Mg2+
Fusobacterium nucleatum subsp. nucleatum
87
-
pyruvate
pH 8.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
90
-
NADH
pH 8.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
98
-
NADH
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
100
-
2-oxobutyrate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
100
-
glyoxylate
pH 7.0, 30°C, recombinant enzyme
Escherichia coli
100
-
pyruvate
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
Fusobacterium nucleatum subsp. nucleatum
110
-
NADH
pH 8.0, 30°C, recombinant enzyme, with Mg2+
Fusobacterium nucleatum subsp. nucleatum
120
-
2-oxoisovalerate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
120
-
phenylpyruvate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
140
-
2-oxobutyrate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
140
-
2-oxovalerate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
160
-
2-oxocaproate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
160
-
Hydroxypyruvate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
200
-
2-oxoisocaproate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
230
-
2-oxocaproate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
240
-
pyruvate
pH 8.0, 30°C, recombinant enzyme; pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
Pseudomonas aeruginosa
270
-
NADH
pH 8.0, 30°C, recombinant enzyme, with or without fructose 1,6-bisphosphate and Mg2+
Pseudomonas aeruginosa
290
-
pyruvate
pH 8.0, 30°C, recombinant enzyme, with Mg2+
Pseudomonas aeruginosa
310
-
NADH
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
370
-
pyruvate
pH 8.0, 30°C, recombinant enzyme, with Mg2+
Escherichia coli
380
-
pyruvate
pH 8.0, 30°C, recombinant enzyme
Escherichia coli
400
-
pyruvate
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
Escherichia coli
400
-
pyruvate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
410
-
oxaloacetate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
410
-
pyruvate
pH 7.0, 30°C, recombinant enzyme
Escherichia coli
420
-
Hydroxypyruvate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
640
-
NADH
pH 7.0, 30°C, recombinant enzyme
Escherichia coli
690
-
NADH
pH 8.0, 30°C, recombinant enzyme, with Mg2+
Escherichia coli
710
-
NADH
pH 8.0, 30°C, recombinant enzyme
Escherichia coli
730
-
NADH
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
Escherichia coli
880
-
glyoxylate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
1100
-
oxaloacetate
pH 7.0, 30°C, recombinant enzyme
Escherichia coli
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
8
assay at
Escherichia coli
7
8
assay at
Fusobacterium nucleatum subsp. nucleatum
7
8
assay at
Pseudomonas aeruginosa
pH Stability
pH Stability
pH Stability Maximum
Commentary
Organism
4
8
purified recombinant His-tagged enzyme, 30°C, 1 h, stable at
Pseudomonas aeruginosa
5
10
purified recombinant His-tagged enzyme, 30°C, 1 h, stable at
Escherichia coli
5
8.5
purified recombinant His-tagged enzyme, 30°C, 1 h, stable at
Fusobacterium nucleatum subsp. nucleatum
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
-
Escherichia coli
NAD+
-
Fusobacterium nucleatum subsp. nucleatum
NAD+
-
Pseudomonas aeruginosa
NADH
-
Escherichia coli
NADH
-
Fusobacterium nucleatum subsp. nucleatum
NADH
-
Pseudomonas aeruginosa
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
additional information
-
additional information
inhibition kinetics
Escherichia coli
additional information
-
additional information
inhibition kinetics
Fusobacterium nucleatum subsp. nucleatum
additional information
-
additional information
inhibition kinetics
Pseudomonas aeruginosa
1.8
-
pyruvate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
5
-
oxaloacetate
pH 7.0, 30°C, recombinant enzyme
Escherichia coli
19
-
Hydroxypyruvate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
20
-
pyruvate
pH 8.0, 30°C, recombinant enzyme, with Mg2+
Pseudomonas aeruginosa
23
-
phenylpyruvate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
44
-
glyoxylate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
140
-
oxaloacetate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
fructose 1,6-bisphosphate
required
Fusobacterium nucleatum subsp. nucleatum
fructose 1,6-bisphosphate
required
Pseudomonas aeruginosa
additional information
no activation of the enzyme by fructose 1,6-bisphosphate and Mg2+
Escherichia coli
Cloned(Commentary) (protein specific)
Commentary
Organism
gene ecd_01352, recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta2 (DE3)
Escherichia coli
gene fn0511, recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta2 (DE3)
Fusobacterium nucleatum subsp. nucleatum
gene pa0927, recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta2 (DE3)
Pseudomonas aeruginosa
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
-
Escherichia coli
NAD+
-
Fusobacterium nucleatum subsp. nucleatum
NAD+
-
Pseudomonas aeruginosa
NADH
-
Escherichia coli
NADH
-
Fusobacterium nucleatum subsp. nucleatum
NADH
-
Pseudomonas aeruginosa
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
glyoxylate
-
Pseudomonas aeruginosa
Hydroxypyruvate
-
Pseudomonas aeruginosa
oxaloacetate
-
Escherichia coli
oxaloacetate
-
Fusobacterium nucleatum subsp. nucleatum
oxamate
constant inhibition at pH 7.0 and pH 8.0
Escherichia coli
oxamate
inhibits the catalytic reaction of FNLDH competitively with pyruvate, but markedly enhances the enzyme reaction at low concentration through canceling of the apparent homotropic cooperativity at pH 8.0
Fusobacterium nucleatum subsp. nucleatum
oxamate
inhibits the catalytic reaction of PALDH in a mixed--type manner at pH 7.0, but markedly enhances the enzyme reaction at low concentration through canceling of the apparent homotropic cooperativity at pH 8.0
Pseudomonas aeruginosa
phenylpyruvate
-
Fusobacterium nucleatum subsp. nucleatum
pyruvate
-
Pseudomonas aeruginosa
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
additional information
-
additional information
inhibition kinetics
Escherichia coli
additional information
-
additional information
inhibition kinetics
Fusobacterium nucleatum subsp. nucleatum
additional information
-
additional information
inhibition kinetics
Pseudomonas aeruginosa
1.8
-
pyruvate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
5
-
oxaloacetate
pH 7.0, 30°C, recombinant enzyme
Escherichia coli
19
-
Hydroxypyruvate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
20
-
pyruvate
pH 8.0, 30°C, recombinant enzyme, with Mg2+
Pseudomonas aeruginosa
23
-
phenylpyruvate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
44
-
glyoxylate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
140
-
oxaloacetate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetics and allosteric mechanism of D-LDHs, overview. The enzyme shows a hyperbolic shaped pyruvate saturation curve below pH 6.5, and shows positive cooperativity in the pyruvate saturation curve above pH 7.5
Escherichia coli
additional information
-
additional information
kinetics and allosteric mechanism of D-LDHs, overview. The enzyme shows a hyperbolic shaped pyruvate saturation curve below pH 6.5, and shows positive cooperativity in the pyruvate saturation curve above pH 7.5
Fusobacterium nucleatum subsp. nucleatum
additional information
-
additional information
kinetics and allosteric mechanism of D-LDHs, overview. The enzyme shows a hyperbolic shaped pyruvate saturation curve below pH 6.5, and shows negative cooperativity in the pyruvate saturation curve above pH 7.5
Pseudomonas aeruginosa
0.019
-
NADH
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
0.022
-
NADH
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
0.028
-
NADH
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
Fusobacterium nucleatum subsp. nucleatum
0.031
-
NADH
pH 8.0, 30°C, recombinant enzyme, with Mg2+
Fusobacterium nucleatum subsp. nucleatum
0.035
-
NADH
pH 8.0, 30°C, recombinant enzyme, with or without fructose 1,6-bisphosphate and Mg2+
Pseudomonas aeruginosa
0.036
-
NADH
pH 8.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
0.055
-
NADH
pH 7.0, 30°C, recombinant enzyme
Escherichia coli
0.088
-
NADH
pH 8.0, 30°C, recombinant enzyme
Escherichia coli
0.09
-
NADH
pH 8.0, 30°C, recombinant enzyme, with Mg2+
Escherichia coli
0.092
-
NADH
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
Escherichia coli
0.1
-
pyruvate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
0.31
-
2-oxobutyrate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
0.34
-
pyruvate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
0.36
-
pyruvate
pH 8.0, 30°C, recombinant enzyme, with Mg2+
Pseudomonas aeruginosa
0.64
-
2-oxobutyrate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
0.68
-
2-oxovalerate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
0.85
-
pyruvate
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
Pseudomonas aeruginosa
1.2
-
pyruvate
pH 8.0, 30°C, recombinant enzyme, with Mg2+
Fusobacterium nucleatum subsp. nucleatum
1.2
-
pyruvate
pH 8.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
1.7
-
oxaloacetate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
1.7
-
pyruvate
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
Fusobacterium nucleatum subsp. nucleatum
2.5
-
oxaloacetate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
2.5
-
pyruvate
pH 8.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
2.6
-
2-oxocaproate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
2.6
-
pyruvate
pH 7.0, 30°C, recombinant enzyme
Escherichia coli
3
-
Hydroxypyruvate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
3.5
-
2-oxoisovalerate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
3.8
-
2-oxoisocaproate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
4
-
2-oxovalerate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
5.8
-
2-oxocaproate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
6.5
-
pyruvate
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
Escherichia coli
6.8
-
glyoxylate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
7.1
-
phenylpyruvate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
7.2
-
pyruvate
pH 8.0, 30°C, recombinant enzyme, with Mg2+
Escherichia coli
7.6
-
pyruvate
pH 8.0, 30°C, recombinant enzyme
Escherichia coli
11
-
phenylpyruvate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
12
-
2-oxoisocaproate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
12
-
Hydroxypyruvate
pH 7.0, 30°C, recombinant enzyme
Escherichia coli
18
-
glyoxylate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
18
-
Hydroxypyruvate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
20
-
glyoxylate
pH 7.0, 30°C, recombinant enzyme
Escherichia coli
30
-
2-oxobutyrate
pH 7.0, 30°C, recombinant enzyme
Escherichia coli
54
-
oxaloacetate
pH 7.0, 30°C, recombinant enzyme
Escherichia coli
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
activates
Fusobacterium nucleatum subsp. nucleatum
Mg2+
activates
Pseudomonas aeruginosa
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
37800
-
-
Pseudomonas aeruginosa
38500
-
-
Escherichia coli
40000
-
4 * 40000, about, sequence calculation
Fusobacterium nucleatum subsp. nucleatum
120000
-
recombinant His-tagged enzyme, gel filtration
Pseudomonas aeruginosa
150000
-
recombinant His-tagged enzyme, peak 2, gel filtration
Escherichia coli
160000
-
recombinant His-tagged enzyme, gel filtration
Fusobacterium nucleatum subsp. nucleatum
330000
-
recombinant His-tagged enzyme, peak 1, gel filtration
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(R)-lactate + NAD+
Fusobacterium nucleatum subsp. nucleatum
-
pyruvate + NADH + H+
-
-
r
(R)-lactate + NAD+
Escherichia coli
-
pyruvate + NADH + H+
-
-
r
pyruvate + NADH + H+
Pseudomonas aeruginosa
-
(R)-lactate + NAD+
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged enzyme from Escherichia coli strain Rosetta2 (DE3) by two different steps of affinity chromatography, and ultrafiltration
Escherichia coli
recombinant His-tagged enzyme from Escherichia coli strain Rosetta2 (DE3) by two different steps of affinity chromatography, and ultrafiltration
Fusobacterium nucleatum subsp. nucleatum
recombinant His-tagged enzyme from Escherichia coli strain Rosetta2 (DE3) by two different steps of affinity chromatography, and ultrafiltration
Pseudomonas aeruginosa
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(R)-lactate + NAD+
-
739841
Fusobacterium nucleatum subsp. nucleatum
pyruvate + NADH + H+
-
-
-
r
(R)-lactate + NAD+
-
739841
Escherichia coli
pyruvate + NADH + H+
-
-
-
r
2-oxobutyrate + NADH + H+
-
739841
Fusobacterium nucleatum subsp. nucleatum
2-hydroxybutyrate + NAD+
-
-
-
r
2-oxobutyrate + NADH + H+
-
739841
Pseudomonas aeruginosa
2-hydroxybutyrate + NAD+
-
-
-
r
2-oxobutyrate + NADH + H+
-
739841
Escherichia coli
2-hydroxybutyrate + NAD+
-
-
-
r
2-oxobutyrate + NADH + H+
-
739841
Fusobacterium nucleatum subsp. nucleatum ATCC 25586 / JCM14847
2-hydroxybutyrate + NAD+
-
-
-
r
2-oxocaproate + NADH + H+
-
739841
Fusobacterium nucleatum subsp. nucleatum
2-hydroxycaproate + NAD+
-
-
-
r
2-oxocaproate + NADH + H+
-
739841
Pseudomonas aeruginosa
2-hydroxycaproate + NAD+
-
-
-
r
2-oxocaproate + NADH + H+
-
739841
Fusobacterium nucleatum subsp. nucleatum ATCC 25586 / JCM14847
2-hydroxycaproate + NAD+
-
-
-
r
2-oxoisocaproate + NADH + H+
-
739841
Fusobacterium nucleatum subsp. nucleatum
2-hydroxyisocaproate + NAD+
-
-
-
r
2-oxoisocaproate + NADH + H+
-
739841
Pseudomonas aeruginosa
2-hydroxyisocaproate + NAD+
-
-
-
r
2-oxoisovalerate + NADH + H+
-
739841
Fusobacterium nucleatum subsp. nucleatum
2-hydroxyisovalerate + NAD+
-
-
-
r
2-oxovalerate + NADH + H+
-
739841
Fusobacterium nucleatum subsp. nucleatum
2-hydroxyvalerate + NAD+
-
-
-
r
2-oxovalerate + NADH + H+
-
739841
Pseudomonas aeruginosa
2-hydroxyvalerate + NAD+
-
-
-
r
glyoxylate + NADH + H+
-
739841
Fusobacterium nucleatum subsp. nucleatum
hydroxyacetate + NAD+
-
-
-
r
glyoxylate + NADH + H+
-
739841
Pseudomonas aeruginosa
hydroxyacetate + NAD+
-
-
-
r
glyoxylate + NADH + H+
-
739841
Escherichia coli
hydroxyacetate + NAD+
-
-
-
r
hydroxypyruvate + NADH + H+
-
739841
Fusobacterium nucleatum subsp. nucleatum
glycerate + NAD+
-
-
-
r
hydroxypyruvate + NADH + H+
-
739841
Pseudomonas aeruginosa
glycerate + NAD+
-
-
-
r
hydroxypyruvate + NADH + H+
-
739841
Escherichia coli
glycerate + NAD+
-
-
-
r
hydroxypyruvate + NADH + H+
-
739841
Fusobacterium nucleatum subsp. nucleatum ATCC 25586 / JCM14847
glycerate + NAD+
-
-
-
r
additional information
the enzyme ECLDH exhibits high substrate specificity toward pyruvate. No or poor activity with 2-oxovalerate, 2-oxoisovalerate, 2-oxocaproate, 2-oxoisocaproate, phenylpyruvate, and hydroxyphenylpyruvate
739841
Escherichia coli
?
-
-
-
-
additional information
the enzyme FNLDH exhibits a broad substrate specificity toward hydrophobic 2-oxoacids such as 2-oxobutyrate and 2-oxovalerate. Poor activity with hydroxyphenylpyruvate and 2-oxoisovalerate
739841
Fusobacterium nucleatum subsp. nucleatum
?
-
-
-
-
additional information
the enzyme PALDH exhibits high substrate specificity toward pyruvate. Poor activity with hydroxyphenylpyruvate and 2-oxoisovalerate
739841
Pseudomonas aeruginosa
?
-
-
-
-
additional information
the enzyme FNLDH exhibits a broad substrate specificity toward hydrophobic 2-oxoacids such as 2-oxobutyrate and 2-oxovalerate. Poor activity with hydroxyphenylpyruvate and 2-oxoisovalerate
739841
Fusobacterium nucleatum subsp. nucleatum ATCC 25586 / JCM14847
?
-
-
-
-
oxaloacetate + NADH + H+
-
739841
Fusobacterium nucleatum subsp. nucleatum
malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
-
739841
Pseudomonas aeruginosa
malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
-
739841
Escherichia coli
malate + NAD+
-
-
-
r
phenylpyruvate + NADH + H+
-
739841
Fusobacterium nucleatum subsp. nucleatum
D-phenyllactate + NAD+
-
-
-
r
phenylpyruvate + NADH + H+
-
739841
Pseudomonas aeruginosa
D-phenyllactate + NAD+
-
-
-
r
pyruvate + NADH + H+
-
739841
Fusobacterium nucleatum subsp. nucleatum
(R)-lactate + NAD+
-
-
-
r
pyruvate + NADH + H+
-
739841
Pseudomonas aeruginosa
(R)-lactate + NAD+
-
-
-
r
pyruvate + NADH + H+
-
739841
Escherichia coli
(R)-lactate + NAD+
-
-
-
r
pyruvate + NADH + H+
-
739841
Fusobacterium nucleatum subsp. nucleatum ATCC 25586 / JCM14847
(R)-lactate + NAD+
-
-
-
r
Subunits (protein specific)
Subunits
Commentary
Organism
homooctamer
8 * 38500, about, sequence calculation, the apparently octameric form of ECLDH is likely an artificial product due to the overexpression, and exhibits slightly but significantly lower specific activity than the tetrameric form
Escherichia coli
homotetramer
4 * 38500, about, sequence calculation
Escherichia coli
homotetramer
4 * 40000, about, sequence calculation
Fusobacterium nucleatum subsp. nucleatum
homotrimer
4 * 37800, about, sequence calculation
Pseudomonas aeruginosa
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Escherichia coli
30
-
assay at
Fusobacterium nucleatum subsp. nucleatum
30
-
assay at
Pseudomonas aeruginosa
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
39
-
purified recombinant His-tagged enzyme, pH 8.0, stable up to
Fusobacterium nucleatum subsp. nucleatum
49
-
purified recombinant His-tagged enzyme, pH 8.0, stable up to
Escherichia coli
57
-
purified recombinant His-tagged enzyme, pH 5.0, stable up to
Pseudomonas aeruginosa
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
11
-
glyoxylate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
18
-
phenylpyruvate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
31
-
2-oxobutyrate
pH 7.0, 30°C, recombinant enzyme
Escherichia coli
39
-
2-oxoisocaproate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
50
-
Hydroxypyruvate
pH 7.0, 30°C, recombinant enzyme
Escherichia coli
69
-
2-oxovalerate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
80
-
NADH
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
Fusobacterium nucleatum subsp. nucleatum
80
-
oxaloacetate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
80
-
pyruvate
pH 7.0, 30°C, recombinant enzyme; pH 8.0, 30°C, recombinant enzyme, with Mg2+
Fusobacterium nucleatum subsp. nucleatum
87
-
pyruvate
pH 8.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
90
-
NADH
pH 8.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
98
-
NADH
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
100
-
2-oxobutyrate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
100
-
glyoxylate
pH 7.0, 30°C, recombinant enzyme
Escherichia coli
100
-
pyruvate
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
Fusobacterium nucleatum subsp. nucleatum
110
-
NADH
pH 8.0, 30°C, recombinant enzyme, with Mg2+
Fusobacterium nucleatum subsp. nucleatum
120
-
2-oxoisovalerate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
120
-
phenylpyruvate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
140
-
2-oxobutyrate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
140
-
2-oxovalerate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
160
-
2-oxocaproate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
160
-
Hydroxypyruvate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
200
-
2-oxoisocaproate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
230
-
2-oxocaproate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
240
-
pyruvate
pH 8.0, 30°C, recombinant enzyme; pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
Pseudomonas aeruginosa
270
-
NADH
pH 8.0, 30°C, recombinant enzyme, with or without fructose 1,6-bisphosphate and Mg2+
Pseudomonas aeruginosa
290
-
pyruvate
pH 8.0, 30°C, recombinant enzyme, with Mg2+
Pseudomonas aeruginosa
310
-
NADH
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
370
-
pyruvate
pH 8.0, 30°C, recombinant enzyme, with Mg2+
Escherichia coli
380
-
pyruvate
pH 8.0, 30°C, recombinant enzyme
Escherichia coli
400
-
pyruvate
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
Escherichia coli
400
-
pyruvate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
410
-
oxaloacetate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
410
-
pyruvate
pH 7.0, 30°C, recombinant enzyme
Escherichia coli
420
-
Hydroxypyruvate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
640
-
NADH
pH 7.0, 30°C, recombinant enzyme
Escherichia coli
690
-
NADH
pH 8.0, 30°C, recombinant enzyme, with Mg2+
Escherichia coli
710
-
NADH
pH 8.0, 30°C, recombinant enzyme
Escherichia coli
730
-
NADH
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
Escherichia coli
880
-
glyoxylate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
1100
-
oxaloacetate
pH 7.0, 30°C, recombinant enzyme
Escherichia coli
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
8
assay at
Escherichia coli
7
8
assay at
Fusobacterium nucleatum subsp. nucleatum
7
8
assay at
Pseudomonas aeruginosa
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
Organism
4
8
purified recombinant His-tagged enzyme, 30°C, 1 h, stable at
Pseudomonas aeruginosa
5
10
purified recombinant His-tagged enzyme, 30°C, 1 h, stable at
Escherichia coli
5
8.5
purified recombinant His-tagged enzyme, 30°C, 1 h, stable at
Fusobacterium nucleatum subsp. nucleatum
General Information
General Information
Commentary
Organism
evolution
although both types of enzymes, NAD-dependent D- and L-lactate dehydrogenases (D-LDH, EC 1.1.1.28; and L-LDH, EC 1.1.1.27) catalyze identical reactions except for the distinct chirality of the lactate product, they are evolutionarily distinct from each other. Allosteric mechanism of D-LDHs, overview
Escherichia coli
evolution
although both types of enzymes, NAD-dependent D- and L-lactate dehydrogenases (D-LDH, EC 1.1.1.28; and L-LDH, EC 1.1.1.27) catalyze identical reactions except for the distinct chirality of the lactate product, they are evolutionarily distinct from each other. Allosteric mechanism of D-LDHs, overview
Fusobacterium nucleatum subsp. nucleatum
evolution
although both types of enzymes, NAD-dependent D- and L-lactate dehydrogenases (D-LDH, EC 1.1.1.28; and L-LDH, EC 1.1.1.27) catalyze identical reactions except for the distinct chirality of the lactate product, they are evolutionarily distinct from each other. Allosteric mechanism of D-LDHs, overview
Pseudomonas aeruginosa
metabolism
the enzyme acts at the last step of the glycolytic pathway under anaerobic conditions
Escherichia coli
metabolism
the enzyme acts at the last step of the glycolytic pathway under anaerobic conditions
Fusobacterium nucleatum subsp. nucleatum
metabolism
the enzyme acts at the last step of the glycolytic pathway under anaerobic conditions
Pseudomonas aeruginosa
General Information (protein specific)
General Information
Commentary
Organism
evolution
although both types of enzymes, NAD-dependent D- and L-lactate dehydrogenases (D-LDH, EC 1.1.1.28; and L-LDH, EC 1.1.1.27) catalyze identical reactions except for the distinct chirality of the lactate product, they are evolutionarily distinct from each other. Allosteric mechanism of D-LDHs, overview
Escherichia coli
evolution
although both types of enzymes, NAD-dependent D- and L-lactate dehydrogenases (D-LDH, EC 1.1.1.28; and L-LDH, EC 1.1.1.27) catalyze identical reactions except for the distinct chirality of the lactate product, they are evolutionarily distinct from each other. Allosteric mechanism of D-LDHs, overview
Fusobacterium nucleatum subsp. nucleatum
evolution
although both types of enzymes, NAD-dependent D- and L-lactate dehydrogenases (D-LDH, EC 1.1.1.28; and L-LDH, EC 1.1.1.27) catalyze identical reactions except for the distinct chirality of the lactate product, they are evolutionarily distinct from each other. Allosteric mechanism of D-LDHs, overview
Pseudomonas aeruginosa
metabolism
the enzyme acts at the last step of the glycolytic pathway under anaerobic conditions
Escherichia coli
metabolism
the enzyme acts at the last step of the glycolytic pathway under anaerobic conditions
Fusobacterium nucleatum subsp. nucleatum
metabolism
the enzyme acts at the last step of the glycolytic pathway under anaerobic conditions
Pseudomonas aeruginosa
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.7
-
glyoxylate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
1
-
2-oxobutyrate
pH 7.0, 30°C, recombinant enzyme
Escherichia coli
2.6
-
phenylpyruvate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
3.2
-
2-oxoisocaproate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
4.2
-
Hydroxypyruvate
pH 7.0, 30°C, recombinant enzyme
Escherichia coli
5.3
-
glyoxylate
pH 7.0, 30°C, recombinant enzyme
Escherichia coli
8.7
-
Hydroxypyruvate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
11
-
phenylpyruvate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
18
-
2-oxovalerate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
21
-
oxaloacetate
pH 7.0, 30°C, recombinant enzyme
Escherichia coli
27
-
2-oxocaproate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
31
-
oxaloacetate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
35
-
2-oxoisovalerate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
35
-
pyruvate
pH 8.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
50
-
pyruvate
pH 8.0, 30°C, recombinant enzyme
Escherichia coli
51
-
pyruvate
pH 8.0, 30°C, recombinant enzyme, with Mg2+
Escherichia coli
53
-
2-oxoisocaproate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
60
-
pyruvate
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
Fusobacterium nucleatum subsp. nucleatum
61
-
pyruvate
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
Escherichia coli
65
-
pyruvate
pH 8.0, 30°C, recombinant enzyme, with Mg2+
Fusobacterium nucleatum subsp. nucleatum
87
-
2-oxocaproate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
130
-
glyoxylate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
140
-
Hydroxypyruvate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
150
-
2-oxobutyrate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
160
-
pyruvate
pH 7.0, 30°C, recombinant enzyme
Escherichia coli
200
-
2-oxovalerate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
200
-
pyruvate
pH 8.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
230
-
oxaloacetate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
230
-
pyruvate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
280
-
pyruvate
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
Pseudomonas aeruginosa
440
-
2-oxobutyrate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
820
-
pyruvate
pH 8.0, 30°C, recombinant enzyme, with Mg2+
Pseudomonas aeruginosa
2500
-
NADH
pH 8.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
2800
-
NADH
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
Fusobacterium nucleatum subsp. nucleatum
3700
-
NADH
pH 8.0, 30°C, recombinant enzyme, with Mg2+
Fusobacterium nucleatum subsp. nucleatum
4000
-
pyruvate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
4400
-
NADH
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
7700
-
NADH
pH 8.0, 30°C, recombinant enzyme, with Mg2+
Escherichia coli
7700
-
NADH
pH 8.0, 30°C, recombinant enzyme; pH 8.0, 30°C, recombinant enzyme, with Mg2+
Pseudomonas aeruginosa
7800
-
NADH
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
Pseudomonas aeruginosa
8000
-
NADH
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
Escherichia coli
8100
-
NADH
pH 8.0, 30°C, recombinant enzyme
Escherichia coli
12000
-
NADH
pH 7.0, 30°C, recombinant enzyme
Escherichia coli
17000
-
NADH
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.7
-
glyoxylate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
1
-
2-oxobutyrate
pH 7.0, 30°C, recombinant enzyme
Escherichia coli
2.6
-
phenylpyruvate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
3.2
-
2-oxoisocaproate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
4.2
-
Hydroxypyruvate
pH 7.0, 30°C, recombinant enzyme
Escherichia coli
5.3
-
glyoxylate
pH 7.0, 30°C, recombinant enzyme
Escherichia coli
8.7
-
Hydroxypyruvate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
11
-
phenylpyruvate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
18
-
2-oxovalerate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
21
-
oxaloacetate
pH 7.0, 30°C, recombinant enzyme
Escherichia coli
27
-
2-oxocaproate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
31
-
oxaloacetate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
35
-
2-oxoisovalerate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
35
-
pyruvate
pH 8.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
50
-
pyruvate
pH 8.0, 30°C, recombinant enzyme
Escherichia coli
51
-
pyruvate
pH 8.0, 30°C, recombinant enzyme, with Mg2+
Escherichia coli
53
-
2-oxoisocaproate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
60
-
pyruvate
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
Fusobacterium nucleatum subsp. nucleatum
61
-
pyruvate
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
Escherichia coli
65
-
pyruvate
pH 8.0, 30°C, recombinant enzyme, with Mg2+
Fusobacterium nucleatum subsp. nucleatum
87
-
2-oxocaproate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
130
-
glyoxylate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
140
-
Hydroxypyruvate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
150
-
2-oxobutyrate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
160
-
pyruvate
pH 7.0, 30°C, recombinant enzyme
Escherichia coli
200
-
2-oxovalerate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
200
-
pyruvate
pH 8.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
230
-
oxaloacetate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
230
-
pyruvate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
280
-
pyruvate
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
Pseudomonas aeruginosa
440
-
2-oxobutyrate
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
820
-
pyruvate
pH 8.0, 30°C, recombinant enzyme, with Mg2+
Pseudomonas aeruginosa
2500
-
NADH
pH 8.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
2800
-
NADH
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
Fusobacterium nucleatum subsp. nucleatum
3700
-
NADH
pH 8.0, 30°C, recombinant enzyme, with Mg2+
Fusobacterium nucleatum subsp. nucleatum
4000
-
pyruvate
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
4400
-
NADH
pH 7.0, 30°C, recombinant enzyme
Fusobacterium nucleatum subsp. nucleatum
7700
-
NADH
pH 8.0, 30°C, recombinant enzyme, with Mg2+
Escherichia coli
7700
-
NADH
pH 8.0, 30°C, recombinant enzyme; pH 8.0, 30°C, recombinant enzyme, with Mg2+
Pseudomonas aeruginosa
7800
-
NADH
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
Pseudomonas aeruginosa
8000
-
NADH
pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate
Escherichia coli
8100
-
NADH
pH 8.0, 30°C, recombinant enzyme
Escherichia coli
12000
-
NADH
pH 7.0, 30°C, recombinant enzyme
Escherichia coli
17000
-
NADH
pH 7.0, 30°C, recombinant enzyme
Pseudomonas aeruginosa
Other publictions for EC 1.1.1.28
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
739831
Yao
-
Efficient biosynthesis of (R)- ...
Staphylococcus epidermidis, Staphylococcus epidermidis ATCC 12228
Adv. Synth. Catal.
358
2923-2928
2016
-
-
1
-
-
-
2
-
-
-
-
2
-
3
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
2
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
740314
Li
Carbon flux trapping: highly e ...
Thermodesulfatator indicus
ChemBioChem
17
1491-1494
2016
-
1
1
-
1
-
-
-
-
2
-
1
-
1
-
-
-
-
-
-
1
-
6
1
1
1
-
-
1
1
-
1
-
-
-
-
1
1
1
-
1
-
-
-
-
-
-
2
-
1
-
-
-
-
-
-
1
-
6
1
1
1
-
-
1
1
-
-
-
-
-
-
-
-
740225
Zhu
Enhancement of phenyllactic ac ...
Lactobacillus pentosus
Biotechnol. Lett.
37
1233-1241
2015
-
-
1
-
3
-
-
-
-
-
-
2
-
3
-
-
-
-
-
-
-
-
3
-
1
-
-
-
1
-
-
2
-
-
-
-
-
1
2
-
3
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
3
-
1
-
-
-
1
-
-
-
-
1
1
-
-
-
740891
Chen
Development of an enzymatic as ...
Rattus norvegicus, Rattus norvegicus Wistar
J. Pharm. Biomed. Anal.
116
150-155
2015
-
-
-
-
-
-
-
-
-
-
-
2
-
3
-
-
-
-
-
1
-
-
4
-
1
-
-
-
1
-
-
3
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
1
-
-
4
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
741246
Zhu
The D-lactate dehydrogenase fr ...
Sporolactobacillus inulinus, Sporolactobacillus inulinus CASD
PLoS ONE
10
e0139066
2015
-
-
1
1
8
-
-
2
-
-
-
-
-
3
-
-
-
1
-
-
1
-
8
1
-
-
-
1
-
-
-
4
-
-
-
-
-
1
4
1
8
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
1
-
8
1
-
-
-
1
-
-
-
-
-
1
1
-
-
-
739810
Kim
Cloning, expression, purificat ...
Lactobacillus jensenii
Acta Crystallogr. Sect. F
70
1046-1048
2014
-
1
1
1
-
-
-
-
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
739841
Furukawa
Diverse allosteric and catalyt ...
Escherichia coli, Fusobacterium nucleatum subsp. nucleatum, Fusobacterium nucleatum subsp. nucleatum ATCC 25586 / JCM14847, Pseudomonas aeruginosa
AMB Express
4
76
2014
3
-
3
-
-
-
9
46
-
2
7
3
-
8
-
-
3
3
-
-
-
-
34
4
3
-
3
41
3
-
3
6
10
-
-
3
-
3
6
-
-
-
-
9
10
46
-
2
7
3
-
-
-
3
-
-
-
-
34
4
3
-
3
41
3
-
3
-
-
6
6
-
44
44
739905
Wang
Major role of NAD-dependent la ...
Bacillus coagulans, Bacillus coagulans 2-6, Lactobacillus delbrueckii subsp. bulgaricus, Lactobacillus delbrueckii subsp. bulgaricus DSM 20081, Lactobacillus plantarum subsp. plantarum, Lactobacillus plantarum subsp. plantarum DSM 20174
Appl. Environ. Microbiol.
80
7134-7141
2014
-
-
3
-
-
-
-
4
-
-
-
8
-
10
-
-
3
-
-
3
3
-
8
-
3
-
-
4
3
-
-
6
-
-
-
-
-
3
6
-
-
-
-
-
-
4
-
-
-
8
-
-
-
3
-
3
3
-
8
-
3
-
-
4
3
-
-
-
-
3
3
-
4
4
740223
Yu
Enzymatic production of D-3-ph ...
Pediococcus pentosaceus
Biotechnol. Lett.
36
627-631
2014
-
1
1
-
1
-
1
-
-
-
-
3
-
5
-
-
1
-
-
-
-
-
4
-
1
1
-
-
1
1
-
2
-
-
-
-
1
1
2
-
1
-
-
1
-
-
-
-
-
3
-
-
-
1
-
-
-
-
4
-
1
1
-
-
1
1
-
-
-
-
-
-
-
-
741291
Sheng
Efficient production of (R)-2- ...
Lactobacillus delbrueckii subsp. bulgaricus, Lactobacillus delbrueckii subsp. bulgaricus ATCC 1184
PLoS ONE
9
e104204
2014
-
-
1
-
1
-
-
-
-
-
-
-
-
5
-
-
-
-
-
-
-
-
2
-
-
-
-
-
1
-
-
1
-
-
-
-
-
1
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
723678
Jun
-
Discovery and characterization ...
Lactobacillus jensenii
Process Biochem.
48
109-117
2013
-
-
1
-
-
-
-
6
-
-
-
1
-
1
-
-
-
-
-
-
15
-
6
-
2
2
4
6
2
2
-
2
-
-
-
-
-
1
2
-
-
-
-
-
-
6
-
-
-
1
-
-
-
-
-
-
15
-
6
-
2
2
4
6
2
2
-
-
-
-
-
-
6
6
740170
Singhvi
Supplementation of medium with ...
Lactobacillus delbrueckii subsp. lactis, Lactobacillus delbrueckii subsp. lactis DSM 20072
Biores. Technol.
146
736-739
2013
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
1
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
1
-
-
-
1
-
-
1
-
-
741405
Zheng
Highly stereoselective biosynt ...
Lactobacillus delbrueckii subsp. bulgaricus, Lactobacillus delbrueckii subsp. bulgaricus ATCC 11842
Sci. Rep.
3
3401
2013
-
-
1
-
4
-
-
4
-
-
-
4
-
4
-
-
1
-
-
-
-
-
11
-
1
-
-
4
1
-
-
2
-
-
-
-
-
1
2
-
4
-
-
-
-
4
-
-
-
4
-
-
-
1
-
-
-
-
11
-
1
-
-
4
1
-
-
-
-
-
-
-
4
4
721879
Yu
Characterization of D-lactate ...
Pediococcus pentosaceus, Pediococcus pentosaceus ATCC 25745
Biosci. Biotechnol. Biochem.
76
853-855
2012
-
-
-
-
-
-
3
2
-
4
1
4
-
4
-
-
-
-
-
-
2
-
4
1
1
1
1
2
1
1
-
2
-
-
-
-
-
-
2
-
-
-
-
3
-
2
-
4
1
4
-
-
-
-
-
-
2
-
4
1
1
1
1
2
1
1
-
-
-
-
-
-
2
2
721909
Mu
Characterization of D-lactate ...
Pediococcus acidilactici, Pediococcus acidilactici DSM 20284
Biotechnol. Lett.
34
907-911
2012
-
-
1
-
-
-
2
2
-
2
1
4
-
2
-
-
1
-
-
-
2
-
4
1
1
1
1
1
1
1
-
2
-
-
-
-
-
1
2
-
-
-
-
2
-
2
-
2
1
4
-
-
-
1
-
-
2
-
4
1
1
1
1
1
1
1
-
-
-
-
-
-
2
2
722140
Li
Characterization of the major ...
Leuconostoc mesenteroides subsp. mesenteroides, Leuconostoc mesenteroides subsp. mesenteroides ATCC 8293
Enzyme Microb. Technol.
51
274-279
2012
-
-
1
-
-
-
3
4
-
-
-
2
-
6
-
-
1
-
-
-
3
-
2
1
2
1
-
2
2
2
-
2
-
-
-
-
-
1
2
-
-
-
-
3
-
4
-
-
-
2
-
-
-
1
-
-
3
-
2
1
2
1
-
2
2
2
-
-
-
-
-
-
-
-
722283
Wienstroer
D-Lactate dehydrogenase as a m ...
Arabidopsis thaliana, Arabidopsis thaliana Columbia-0
FEBS Lett.
586
36-40
2012
-
1
-
-
1
-
-
-
-
-
-
2
-
5
-
-
-
-
-
2
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
1
-
2
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
2
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
721200
Shibahara
Crystallization and preliminar ...
Aeropyrum pernix
Acta Crystallogr. Sect. F
67
1425-1427
2011
-
-
1
1
-
-
-
-
-
-
2
2
-
1
-
-
1
-
-
-
-
-
2
1
-
-
-
-
-
-
-
2
-
-
-
-
-
1
2
1
-
-
-
-
-
-
-
-
2
2
-
-
-
1
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
701818
Okano
Improved production of homo-D- ...
Lactobacillus plantarum, Lactobacillus plantarum NCIMB 8826
Appl. Environ. Microbiol.
75
7858-7861
2009
-
-
-
-
1
-
-
-
-
-
-
3
-
4
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
710727
Antonyuk
Structure of D-lactate dehydro ...
Aquifex aeolicus
Acta Crystallogr. Sect. F
65
1209-1213
2009
-
-
1
1
-
-
-
-
-
-
-
1
-
3
-
-
1
-
-
-
-
-
3
1
-
-
-
-
-
-
-
3
-
-
-
-
-
1
3
1
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
3
1
-
-
-
-
-
-
-
-
-
1
1
-
-
-
684633
Okino
Production of D-lactic acid by ...
Escherichia coli, Lactobacillus delbrueckii
Appl. Microbiol. Biotechnol.
78
449-454
2008
-
-
2
-
-
-
-
-
-
4
-
2
-
5
-
-
-
-
-
-
2
-
4
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
4
-
2
-
-
-
-
-
-
2
-
4
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
695707
Xu
Breeding of D(-)-lactic acid h ...
Sporolactobacillus sp., Sporolactobacillus sp. DX12
Appl. Biochem. Biotechnol.
160
314-321
2008
-
-
-
-
1
-
-
-
-
-
-
2
-
2
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
688878
Mazzei
-
Peroxidase based biosensors fo ...
Staphylococcus epidermidis
Microchem. J.
87
81-86
2007
-
1
-
-
1
-
-
-
-
1
-
1
-
1
-
-
-
-
-
1
1
-
1
-
1
-
-
-
1
-
-
2
-
-
-
-
1
-
2
-
1
-
-
-
-
-
-
1
-
1
-
-
-
-
-
1
1
-
1
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
667751
Minenko
Use of the addressing sequence ...
Saccharomyces cerevisiae
Biochemistry
71
32-38
2006
-
-
1
-
-
-
-
-
2
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
669543
Ishida
D-lactic acid production by me ...
Leuconostoc mesenteroides
J. Biosci. Bioeng.
101
172-177
2006
-
1
1
-
-
-
-
-
-
-
-
-
-
5
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
665878
Fujisawa
-
D-lactate metabolism in starve ...
Amphioctopus fangsiao
J. Exp. Zool. A
303A
489-496
2005
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
668233
Findrik
-
Modelling and optimization of ...
Lactobacillus leichmannii
Chem. Biochem. Eng. Q.
19
351-358
2005
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
669152
Ishikura
Recognition site for the side ...
Lactobacillus pentosus
J. Biochem.
138
741-749
2005
-
-
-
-
9
-
-
46
-
-
-
-
-
2
-
-
-
-
-
-
-
-
10
-
-
-
-
46
-
-
-
1
-
-
-
-
-
-
1
-
9
-
-
-
-
46
-
-
-
-
-
-
-
-
-
-
-
-
10
-
-
-
-
46
-
-
-
-
-
-
-
-
-
-
669327
Shinoda
Distinct conformation-mediated ...
Lactobacillus pentosus
J. Biol. Chem.
280
17068-17075
2005
-
-
-
1
-
-
2
8
-
-
-
-
-
3
-
-
-
-
-
-
-
-
4
-
-
-
-
8
-
-
-
-
4
-
-
-
-
-
-
1
-
-
-
2
4
8
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
8
-
-
-
-
-
-
-
-
-
-
670130
Zhu
Effect of a single-gene knocko ...
Escherichia coli
Metab. Eng.
7
104-115
2005
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
654456
Hachiya
Interaction of D-lactate dehyd ...
Saccharomyces cerevisiae
Biochem. Biophys. Res. Commun.
319
78-82
2004
-
-
-
-
1
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
655064
Horikiri
Electron acquisition system co ...
Rhodopseudomonas palustris
Biosci. Biotechnol. Biochem.
68
516-522
2004
-
-
-
-
-
-
1
1
-
-
2
-
-
2
-
-
1
-
-
-
1
-
3
1
1
-
2
-
1
-
-
2
1
1
-
-
-
-
2
-
-
-
-
1
1
1
-
-
2
-
-
-
-
1
-
-
1
-
3
1
1
-
2
-
1
-
-
1
-
-
-
-
-
-
656426
Iino
The effect of sodium acetate o ...
Lactobacillus plantarum, Lactobacillus plantarum 39 / NRIC 1067 / ATCC 14917 / DSM 20174, Lactobacillus sakei, Lactobacillus sakei NRIC 1071 / ATCC 15521 / NCIMB 1071
J. Gen. Appl. Microbiol.
49
51-58
2003
-
-
-
-
-
-
-
-
2
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
656314
Isobe
Crystallization and some prope ...
Staphylococcus sp., Staphylococcus sp. LDH-1
J. Biosci. Bioeng.
94
330-335
2002
-
-
-
-
-
-
3
4
-
-
2
-
-
3
-
-
1
-
-
-
1
-
11
2
1
1
-
-
2
-
1
2
-
1
-
-
-
-
2
-
-
-
-
3
-
4
-
-
2
-
-
-
-
1
-
-
1
-
11
2
1
1
-
-
2
-
1
1
-
-
-
-
-
-
656500
Razeto
Domain closure, substrate spec ...
Lactobacillus delbrueckii subsp. bulgaricus
J. Mol. Biol.
318
109-119
2002
-
-
-
1
1
-
-
-
-
-
-
-
-
3
-
-
-
1
-
-
-
-
2
-
-
-
-
-
2
-
-
2
-
-
-
-
-
-
2
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
286501
Kochhar
Roles of His205, His296, His30 ...
Lactobacillus delbrueckii subsp. bulgaricus
Eur. J. Biochem.
267
1633-1639
2000
-
-
-
-
4
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286502
Dym
The crystal structure of D-lac ...
Escherichia coli
Proc. Natl. Acad. Sci. USA
97
9413-9418
2000
-
-
-
1
-
-
-
-
2
-
-
1
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
1
-
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286500
Stoll
A thioredoxin fusion protein o ...
Enterococcus faecium
Protein Sci.
7
1147-1155
1998
3
-
1
1
-
-
-
3
-
-
-
1
-
3
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
3
-
1
2
1
-
-
-
-
-
3
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286499
Dartois
Purification, properties and D ...
Leuconostoc mesenteroides subsp. cremoris
Res. Microbiol.
146
291-302
1995
-
-
1
-
-
-
-
4
-
-
1
1
-
4
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
2
-
-
-
-
-
1
2
-
-
-
-
-
-
4
-
-
1
1
-
-
-
1
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286503
Nessler
Crystallization of D-lactate d ...
Lactobacillus delbrueckii subsp. bulgaricus
J. Mol. Biol.
235
370-371
1994
-
-
-
1
-
-
-
-
-
-
-
1
-
2
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286498
Erwin
Oxidation of D-lactate and L-l ...
Neisseria meningitidis
J. Bacteriol.
175
6382-6391
1993
-
-
1
-
-
-
9
1
1
2
1
1
-
3
-
-
1
-
-
-
-
-
1
-
-
-
-
-
1
-
-
2
-
-
-
-
-
1
2
-
-
-
-
9
-
1
1
2
1
1
-
-
-
1
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
286496
Kochhar
Primary structure, physicochem ...
Lactobacillus delbrueckii subsp. bulgaricus
J. Biol. Chem.
267
8499-8513
1992
-
-
-
-
-
-
-
-
-
-
1
1
-
2
-
-
1
-
-
-
-
-
1
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
1
-
-
-
-
1
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
286497
Kochhar
Cloning and overexpression of ...
Lactobacillus delbrueckii subsp. bulgaricus
Biochem. Biophys. Res. Commun.
185
705-712
1992
-
-
1
-
-
-
-
2
-
-
1
1
-
5
-
-
1
-
-
-
1
-
2
1
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
2
-
-
1
1
-
-
-
1
-
-
1
-
2
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
286504
Kochhar
Glutamate 264 modulates the pH ...
Lactobacillus delbrueckii subsp. bulgaricus
J. Biol. Chem.
267
20298-20301
1992
-
-
1
-
1
-
-
4
-
-
-
1
-
3
-
-
1
-
-
-
-
-
4
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
4
-
-
-
1
-
-
-
1
-
-
-
-
4
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
659546
Schmidt
Optimization of a process for ...
Staphylococcus epidermidis
J. Biotechnol.
24
315-327
1992
-
1
-
-
-
1
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
1
-
-
-
1
-
-
1
-
-
-
-
1
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
286495
Le Bras
Properties of D-lactate dehydr ...
Lactobacillus delbrueckii subsp. bulgaricus
FEMS Microbiol. Lett.
79
89-93
1991
-
-
-
-
-
-
-
2
-
-
2
1
-
2
-
-
1
-
-
-
1
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
2
1
-
-
-
1
-
-
1
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286483
Jaenicke
-
Dimeric lactic dehydrogenase f ...
Cerastoderma edule
Naturwissenschaften
68
205-206
1981
-
-
-
-
-
-
-
-
-
-
2
1
-
1
-
-
-
-
-
2
-
-
1
1
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
2
1
-
-
-
-
-
2
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286430
Garvie
Bacterial lactate dehydrogenas ...
Escherichia coli, Eubacterium limosum, Klebsiella aerogenes, Lactobacillus acidophilus, Lactobacillus brevis, Lactobacillus buchneri, Lactobacillus casei, Lactobacillus delbrueckii, Lactobacillus delbrueckii subsp. bulgaricus, Lactobacillus delbrueckii subsp. lactis, Lactobacillus fermentum, Lactobacillus jensenii, Lactobacillus jugurt-helveticus, Lactobacillus leichmannii, Lactobacillus plantarum, Lactobacillus vermiforme, Lactococcus lactis, Leuconostoc lactis, Leuconostoc mesenteroides, Leuconostoc mesenteroides subsp. cremoris, Leuconostoc mesenteroides subsp. dextranicum, Mammalia, Mycoplasma sp., Oenococcus oeni, Pediococcus acidilactici, Pediococcus damnosus, Pediococcus inopinatus, Pediococcus pentosaceus, Selenomonas ruminantium, Staphylococcus aureus, Staphylococcus haemolyticus, Staphylococcus hominis, Staphylococcus sp., Staphylococcus warneri, Weissella confusa, Weissella paramesenteroides, Weissella viridescens
Microbiol. Rev.
44
106-139
1980
-
-
-
-
-
-
197
11
-
-
-
37
-
37
-
-
-
-
-
-
-
-
37
-
-
-
15
-
8
-
-
74
-
-
-
-
-
-
74
-
-
-
-
197
-
11
-
-
-
37
-
-
-
-
-
-
-
-
37
-
-
-
15
-
8
-
-
-
-
-
-
-
-
-
286489
Long
-
Comparative enzymology and phy ...
Haliotis cracherodii, Helix aspersa
J. Exp. Zool.
207
237-248
1979
-
-
-
-
-
-
2
10
-
-
-
2
-
2
-
-
2
-
-
2
-
-
4
2
-
-
-
-
4
-
-
4
-
-
-
-
-
-
4
-
-
-
-
2
-
10
-
-
-
2
-
-
-
2
-
2
-
-
4
2
-
-
-
-
4
-
-
-
-
-
-
-
-
-
286488
Storey
Lactate dehydrogenase in tissu ...
Helix aspersa
Comp. Biochem. Physiol. B
56
181-187
1977
-
-
-
-
-
-
1
4
-
-
2
1
-
2
-
-
-
-
-
5
-
-
1
1
-
-
-
-
2
-
-
2
-
-
-
-
-
-
2
-
-
-
-
1
-
4
-
-
2
1
-
-
-
-
-
5
-
-
1
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
286484
LeJohn
D(-)-lactate dehydrogenase fro ...
Phytophthora undulata, Pythium debaryanum, Sapromyces elongatus
Methods Enzymol.
41B
293-298
1975
3
-
-
-
-
-
-
-
-
-
2
3
-
3
-
-
3
3
-
3
-
6
3
-
-
-
-
-
-
-
-
6
-
-
-
3
-
-
6
-
-
-
-
-
-
-
-
-
2
3
-
-
-
3
-
3
-
6
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286490
Wittenberger
D(-)-Lactate dehydrogenase fro ...
Eubacterium limosum
Methods Enzymol.
41B
299-303
1975
-
-
-
-
-
1
4
-
-
-
1
1
-
1
-
-
1
-
-
-
-
1
1
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
2
-
-
1
-
4
-
-
-
-
1
1
-
-
-
1
-
-
-
1
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
286491
Long
D-Lactate dehydrogenase from t ...
Limulus polyphemus
Methods Enzymol.
41B
313-323
1975
-
-
-
-
-
1
4
4
-
-
2
1
-
1
-
-
1
-
-
1
-
-
1
1
-
-
2
1
-
-
-
2
-
-
-
-
-
-
2
-
-
1
-
4
-
4
-
-
2
1
-
-
-
1
-
1
-
-
1
1
-
-
2
1
-
-
-
-
-
-
-
-
-
-
286492
Long
Diphosphopyridine nucleotide-l ...
Alitta virens, Limulus polyphemus
Arch. Biochem. Biophys.
154
696-710
1973
-
-
-
-
-
-
2
-
-
-
2
2
-
2
-
-
2
-
-
-
-
-
2
1
-
-
-
-
-
-
-
4
-
-
-
-
-
-
4
-
-
-
-
2
-
-
-
-
2
2
-
-
-
2
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286493
Purohit
D(-)-lactate dehydrogenase fro ...
Allomyces sp.
Arch. Mikrobiol.
84
287-300
1972
-
-
-
-
-
1
2
-
-
-
-
1
-
1
-
-
1
-
-
-
-
1
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
1
-
2
-
-
-
-
-
1
-
-
-
1
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286485
Garland
Salt-induced alteration of D(- ...
Heterostelium pallidum
Biochem. Biophys. Res. Commun.
26
679-685
1967
-
-
-
-
-
-
1
-
-
-
-
1
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286486
Wolin
Fructose-1,6-diphosphate requi ...
Streptococcus equinus
Science
146
775-776
1964
1
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
1
-
-
2
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286487
Pascal
-
Sur la configuration du lactat ...
Klebsiella aerogenes
Ann. Inst. Pasteur (Paris)
107
55-62
1964
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-