BRENDA - Enzyme Database show
show all sequences of 1.1.1.363

Simultaneous analysis of NAD- and NADP-linked activities of dual nucleotide-specific dehydrogenases. Application to Leuconostoc mesenteroides glucose-6-phosphate dehydrogenase

Levy, H.R.; Daouk, G.H.; J. Biol. Chem. 254, 4843-4837 (1997)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
ATP
inhibits competitively with respect to thionicotinamide-NAD+
Leuconostoc mesenteroides
D-glucose 6-phosphate
high concentrations inhibit the NADP+-linked reaction in the dual wavelength assay (a method employing a mixture of one coenzyme and the thionicotinamide analog of the other coenzyme). Such inhibition is not observed in conventional assays using either NADP+ or thionicotinamide-NADP+
Leuconostoc mesenteroides
NADH
inhibits noncompetitively with respect to thionicotinamide-NAD+
Leuconostoc mesenteroides
NADPH
inhibits competitively with respect to thionicotinamide-NADP+
Leuconostoc mesenteroides
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.001
-
thionicotinamide-NADP+
pH 7.8, 25°C
Leuconostoc mesenteroides
0.006
-
NADP+
pH 7.8, 25°C
Leuconostoc mesenteroides
0.007
-
D-glucose 6-phosphate
pH 7.8, 25°C, cosubstrate: thionicotinamide-NAD+
Leuconostoc mesenteroides
0.009
-
D-glucose 6-phosphate
pH 7.8, 25°C, cosubstrate: thionicotinamide-NADP+
Leuconostoc mesenteroides
0.011
-
thionicotinamide-NAD+
pH 7.8, 25°C
Leuconostoc mesenteroides
0.053
-
D-glucose 6-phosphate
pH 7.8, 25°C, cosubstrate: NAD+
Leuconostoc mesenteroides
0.081
-
D-glucose 6-phosphate
pH 7.8, 25°C, cosubstrate: NADP+
Leuconostoc mesenteroides
0.106
-
NAD+
pH 7.8, 25°C
Leuconostoc mesenteroides
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Leuconostoc mesenteroides
-
-
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
a method is described which enables one to assay simultaneously the NAD+- and NADP+-linked reactions of dehydrogenases which can utilize both coenzymes. The method is based on the fact that the thionicotinamide analogs of NADH and NADPH absorb light maximally at 400 nm, a wavelength sufficiently far removed from the absorbance maximum of NADH and NADPH to permit measurements of the simultaneous reduction of NAD+ (or NADP+) and the thionicotinamide analog of NADP+ (or NAD+). Application of the method to glucosed 6-phosphate dehydrogenase from Leuconostoc mesenteroides reveals differential effects of glucose 6-phosphate concentration on the NAD+- and NADP+-linked reactions catalyzed by this enzyme which can not be detected by conventional assay procedures and which may have regulatory significance
Leuconostoc mesenteroides
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-glucose 6-phosphate + NAD+
iso ordered bi bi reaction
722581
Leuconostoc mesenteroides
6-phospho-D-glucono-1,5-lactone + NADH + H+
-
-
-
?
D-glucose 6-phosphate + NADP+
ordered bi bi reaction
722581
Leuconostoc mesenteroides
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
?
D-glucose 6-phosphate + thionicotinamide-NAD+
-
722581
Leuconostoc mesenteroides
6-phospho-D-glucono-1,5-lactone + thionicotinamide-NADH + H+
-
-
-
?
D-glucose 6-phosphate + thionicotinamide-NADP+
-
722581
Leuconostoc mesenteroides
6-phospho-D-glucono-1,5-lactone + thionicotinamide-NADPH + H+
-
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
-
Leuconostoc mesenteroides
NADP+
-
Leuconostoc mesenteroides
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
-
Leuconostoc mesenteroides
NADP+
-
Leuconostoc mesenteroides
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
ATP
inhibits competitively with respect to thionicotinamide-NAD+
Leuconostoc mesenteroides
D-glucose 6-phosphate
high concentrations inhibit the NADP+-linked reaction in the dual wavelength assay (a method employing a mixture of one coenzyme and the thionicotinamide analog of the other coenzyme). Such inhibition is not observed in conventional assays using either NADP+ or thionicotinamide-NADP+
Leuconostoc mesenteroides
NADH
inhibits noncompetitively with respect to thionicotinamide-NAD+
Leuconostoc mesenteroides
NADPH
inhibits competitively with respect to thionicotinamide-NADP+
Leuconostoc mesenteroides
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.001
-
thionicotinamide-NADP+
pH 7.8, 25°C
Leuconostoc mesenteroides
0.006
-
NADP+
pH 7.8, 25°C
Leuconostoc mesenteroides
0.007
-
D-glucose 6-phosphate
pH 7.8, 25°C, cosubstrate: thionicotinamide-NAD+
Leuconostoc mesenteroides
0.009
-
D-glucose 6-phosphate
pH 7.8, 25°C, cosubstrate: thionicotinamide-NADP+
Leuconostoc mesenteroides
0.011
-
thionicotinamide-NAD+
pH 7.8, 25°C
Leuconostoc mesenteroides
0.053
-
D-glucose 6-phosphate
pH 7.8, 25°C, cosubstrate: NAD+
Leuconostoc mesenteroides
0.081
-
D-glucose 6-phosphate
pH 7.8, 25°C, cosubstrate: NADP+
Leuconostoc mesenteroides
0.106
-
NAD+
pH 7.8, 25°C
Leuconostoc mesenteroides
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
a method is described which enables one to assay simultaneously the NAD+- and NADP+-linked reactions of dehydrogenases which can utilize both coenzymes. The method is based on the fact that the thionicotinamide analogs of NADH and NADPH absorb light maximally at 400 nm, a wavelength sufficiently far removed from the absorbance maximum of NADH and NADPH to permit measurements of the simultaneous reduction of NAD+ (or NADP+) and the thionicotinamide analog of NADP+ (or NAD+). Application of the method to glucosed 6-phosphate dehydrogenase from Leuconostoc mesenteroides reveals differential effects of glucose 6-phosphate concentration on the NAD+- and NADP+-linked reactions catalyzed by this enzyme which can not be detected by conventional assay procedures and which may have regulatory significance
Leuconostoc mesenteroides
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-glucose 6-phosphate + NAD+
iso ordered bi bi reaction
722581
Leuconostoc mesenteroides
6-phospho-D-glucono-1,5-lactone + NADH + H+
-
-
-
?
D-glucose 6-phosphate + NADP+
ordered bi bi reaction
722581
Leuconostoc mesenteroides
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
?
D-glucose 6-phosphate + thionicotinamide-NAD+
-
722581
Leuconostoc mesenteroides
6-phospho-D-glucono-1,5-lactone + thionicotinamide-NADH + H+
-
-
-
?
D-glucose 6-phosphate + thionicotinamide-NADP+
-
722581
Leuconostoc mesenteroides
6-phospho-D-glucono-1,5-lactone + thionicotinamide-NADPH + H+
-
-
-
?
Other publictions for EC 1.1.1.363
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)
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1
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2
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4
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2
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2
2
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1
2
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2
2
4
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4
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1
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4
5
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6
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5
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11
-
1
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4
1
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4
3
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1
4
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4
3
5
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6
-
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-
5
-
11
-
1
-
-
4
1
-
-
-
-
1
1
-
2
2
722852
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-
-
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-
-
-
-
1
-
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1
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1
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1
1
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1
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3
1
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1
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1
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1
1
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1
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Leuconostoc mesenteroides
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220-228
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2
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2
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1
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1
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1
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Leuconostoc mesenteroides
Acta Crystallogr. Sect. D
57
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-
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1
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1
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1
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721583
Cosgrove
An examination of the role of ...
Leuconostoc mesenteroides
Biochemistry
39
15002-15011
2000
-
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1
1
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1
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1
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1
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1
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1
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1
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721584
Vought
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Leuconostoc mesenteroides
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39
15012-15021
2000
-
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-
14
-
1
54
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2
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1
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2
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1
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54
1
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11
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14
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1
11
54
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2
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2
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1
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54
1
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55
55
721580
Cosgrove
On the mechanism of the reacti ...
Leuconostoc mesenteroides
Biochemistry
37
2759-2767
1998
-
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1
3
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1
12
-
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2
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1
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1
1
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2
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1
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12
1
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2
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1
3
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1
2
12
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2
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1
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2
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1
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12
1
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12
12
722581
Levy
Simultaneous analysis of NAD- ...
Leuconostoc mesenteroides
J. Biol. Chem.
254
4843-4837
1997
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4
8
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721411
Levy
Identification of an arginine ...
Leuconostoc mesenteroides
Arch. Biochem. Biophys.
326
145-151
1996
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1
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3
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1
15
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1
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1
1
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10
1
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2
4
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1
2
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3
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1
4
15
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3
1
1
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10
1
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19
19
721408
Szweda
Oxidative modification of gluc ...
Leuconostoc mesenteroides
Arch. Biochem. Biophys.
301
391-395
1993
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2
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721695
Plomer
Renaturation of glucose-6-phos ...
Leuconostoc mesenteroides
Biochim. Biophys. Acta
1163
89-96
1993
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722594
Szweda
Inactivation of glucose-6-phos ...
Leuconostoc mesenteroides
J. Biol. Chem.
268
3342-3347
1993
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1
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723730
Adams
Site-directed mutagenesis to f ...
Leuconostoc mesenteroides
Protein Sci.
2
859-662
1993
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1
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1
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1
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2
1
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-
-
2
-
1
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1
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721694
Plomer
Denaturation of glucose-6-phos ...
Leuconostoc mesenteroides
Biochim. Biophys. Acta
1122
234-242
1992
-
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-
-
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1
1
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722593
Szweda
Iron-catalyzed oxidative modif ...
Leuconostoc mesenteroides
J. Biol. Chem.
267
3096-3100
1992
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2
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2
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-
723718
Lee
Lysine-21 of Leuconostoc mesen ...
Leuconostoc mesenteroides
Protein Sci.
1
329-334
1992
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-
1
-
2
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1
11
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2
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1
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1
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1
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2
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1
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12
1
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2
3
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1
2
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2
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1
3
11
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2
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1
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1
-
2
-
1
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12
1
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8
8
722589
Lee
Cloning of the gene and amino ...
Leuconostoc mesenteroides
J. Biol. Chem.
266
13028-13034
1991
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1
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1
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4
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1
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1
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722590
LaDine
Interaction of Leuconostoc mes ...
Leuconostoc mesenteroides
J. Biol. Chem.
266
5558-5562
1991
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2
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2
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1
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2
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1
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1
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2
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2
2
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2
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-
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2
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1
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1
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721573
Crans
Vanadate dimer and tetramer bo ...
Leuconostoc mesenteroides
Biochemistry
29
6698-6706
1990
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1
4
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1
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1
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1
1
4
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2
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721406
Kurlandsky
Glucose-6-phosphate dehydrogen ...
Leuconostoc mesenteroides
Arch. Biochem. Biophys.
264
93-102
1988
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4
1
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1
1
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2
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1
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2
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2
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4
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1
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1
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2
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1
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722476
Murphy
Expression of the gene for NAD ...
Leuconostoc mesenteroides
J. Bacteriol.
169
334-339
1987
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1
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2
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722585
White
Modification of glucose-6-phos ...
Leuconostoc mesenteroides
J. Biol. Chem.
262
1223-1229
1987
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-
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1
1
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1
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1
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1
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1
1
1
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1
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721402
Levy
Glucose-6-phosphate dehydrogen ...
Leuconostoc mesenteroides
Arch. Biochem. Biophys.
222
473-488
1983
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4
12
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2
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1
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4
-
1
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2
8
-
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2
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4
8
12
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2
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4
-
1
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722582
Adams
Crystallization and preliminar ...
Leuconostoc mesenteroides
J. Biol. Chem.
258
5867-5868
1983
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1
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1
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1
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721569
Haghighi
Glucose-6-phosphate dehydrogen ...
Leuconostoc mesenteroides
Biochemistry
21
6421-6428
1982
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1
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2
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721570
Haghighi
Glucose-6-phosphate dehydrogen ...
Leuconostoc mesenteroides
Biochemistry
21
6429-6434
1982
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-
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4
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1
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1
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2
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4
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1
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2
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721401
Levy
Regulation of coenzyme utiliza ...
Leuconostoc mesenteroides
Arch. Biochem. Biophys.
198
406-413
1979
2
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5
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2
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1
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2
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2
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2
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2
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5
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2
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2
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721400
Grove
Glucose-6-phosphate dehydrogen ...
Leuconostoc mesenteroides
Arch. Biochem. Biophys.
17
307-316
1976
-
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10
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2
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1
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1
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2
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2
9
-
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2
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-
10
9
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2
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1
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2
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721511
Coe
Acyl coenzyme A inhibition of ...
Leuconostoc mesenteroides
Biochem. Biophys. Res. Commun.
53
66-69
1973
-
-
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5
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1
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2
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2
5
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2
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5
5
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2
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722578
Olive
Glucose 6-phosphate dehydrogen ...
Leuconostoc mesenteroides
J. Biol. Chem.
246
2047-2057
1971
-
-
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4
9
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2
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1
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8
-
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2
1
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2
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4
1
9
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2
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8
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