BRENDA - Enzyme Database show
show all sequences of 1.1.1.363

Site directed immobilization of glucose-6-phosphate dehydrogenase via thiol-disulfide interchange: influence on catalytic activity of cysteines introduced at different positions

Simons, J.R.; Mosisch, M.; Torda, A.E.; Hilterhaus, L.; J. Biotechnol. 167, 1-7 (2013)

Data extracted from this reference:

Engineering
Amino acid exchange
Commentary
Organism
D205C
enzyme variant with cysteine close to the dimer interface, about 30% loss of specific activity compared to wild-type enzymeshows changes in activity and the efficacy of immobilization.
Leuconostoc mesenteroides
D453C
enzyme variant with cysteine far from the active center, no significant loss in specific activity compared to wild-type enzyme, in contrast to wild-type enzyme, the mutant enzyme is readily immobilited
Leuconostoc mesenteroides
L218C
enzyme variant with cysteine close to the active center, about 30% loss of specific activity compared to wild-type enzyme, the mutant enzyme shows almost complete immobilization but poor carrier activity
Leuconostoc mesenteroides
General Stability
General Stability
Organism
eluted mutant enzyme D453C shows almost double the activity of the immobilized enzyme, which is consistent with 49% activity loss due to immobilization. Mutant enzyme D205C produces a 1.8-fold higher activity compared to its immobilized state. Eluted mutant enzyme L218C shows 9.9 times the activity of its immobilized state
Leuconostoc mesenteroides
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
69000
-
x * 69000, SDS-PAGE
Leuconostoc mesenteroides
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Leuconostoc mesenteroides
-
-
-
Storage Stability
Storage Stability
Organism
4°C, 8 months, enzym variants L218C, D205C or D453C, no loss of activity
Leuconostoc mesenteroides
Subunits
Subunits
Commentary
Organism
?
x * 69000, SDS-PAGE
Leuconostoc mesenteroides
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Leuconostoc mesenteroides
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Leuconostoc mesenteroides
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
D205C
enzyme variant with cysteine close to the dimer interface, about 30% loss of specific activity compared to wild-type enzymeshows changes in activity and the efficacy of immobilization.
Leuconostoc mesenteroides
D453C
enzyme variant with cysteine far from the active center, no significant loss in specific activity compared to wild-type enzyme, in contrast to wild-type enzyme, the mutant enzyme is readily immobilited
Leuconostoc mesenteroides
L218C
enzyme variant with cysteine close to the active center, about 30% loss of specific activity compared to wild-type enzyme, the mutant enzyme shows almost complete immobilization but poor carrier activity
Leuconostoc mesenteroides
General Stability (protein specific)
General Stability
Organism
eluted mutant enzyme D453C shows almost double the activity of the immobilized enzyme, which is consistent with 49% activity loss due to immobilization. Mutant enzyme D205C produces a 1.8-fold higher activity compared to its immobilized state. Eluted mutant enzyme L218C shows 9.9 times the activity of its immobilized state
Leuconostoc mesenteroides
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
69000
-
x * 69000, SDS-PAGE
Leuconostoc mesenteroides
Storage Stability (protein specific)
Storage Stability
Organism
4°C, 8 months, enzym variants L218C, D205C or D453C, no loss of activity
Leuconostoc mesenteroides
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 69000, SDS-PAGE
Leuconostoc mesenteroides
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Leuconostoc mesenteroides
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Leuconostoc mesenteroides
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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2
4
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4
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43
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742533
Olavarria
Quantifying NAD(P)H productio ...
Pseudomonas putida, Pseudomonas putida KT 2240
FEBS open bio
5
908-915
2015
-
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1
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4
5
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6
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3
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5
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11
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1
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4
1
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1
1
-
2
2
722852
Simons
Site directed immobilization o ...
Leuconostoc mesenteroides
J. Biotechnol.
167
1-7
2013
-
-
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-
3
1
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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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740878
Cumana
-
Immobilization of glucose 6-ph ...
Leuconostoc mesenteroides
J. Mol. Catal. B
85-86
220-228
2013
-
-
-
-
-
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2
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2
-
1
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2
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723154
Ravera
Oligomerization studies of Leu ...
Leuconostoc mesenteroides
Mol. Biol.
44
472-476
2010
-
-
-
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-
1
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1
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-
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721145
Naylor
NADP+ and NAD+ binding to the ...
Leuconostoc mesenteroides
Acta Crystallogr. Sect. D
57
635-648
2001
-
-
-
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
-
-
-
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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1
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1
-
-
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-
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-
721584
Vought
Delineation of the roles of am ...
Leuconostoc mesenteroides
Biochemistry
39
15012-15021
2000
-
-
-
-
14
-
1
54
-
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-
2
-
1
-
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-
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2
-
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
-
1
-
-
54
1
-
-
-
-
-
-
-
55
55
721580
Cosgrove
On the mechanism of the reacti ...
Leuconostoc mesenteroides
Biochemistry
37
2759-2767
1998
-
-
-
1
3
-
1
12
-
-
-
2
-
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
-
1
-
-
12
1
-
-
-
-
-
-
-
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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1
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8
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1
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721411
Levy
Identification of an arginine ...
Leuconostoc mesenteroides
Arch. Biochem. Biophys.
326
145-151
1996
-
-
1
-
3
-
1
15
-
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1
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3
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
-
-
10
1
-
-
-
-
-
-
-
19
19
721408
Szweda
Oxidative modification of gluc ...
Leuconostoc mesenteroides
Arch. Biochem. Biophys.
301
391-395
1993
-
-
-
-
-
-
2
-
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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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1
1
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1
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-
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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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1
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723730
Adams
Site-directed mutagenesis to f ...
Leuconostoc mesenteroides
Protein Sci.
2
859-662
1993
-
-
-
1
-
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-
-
-
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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
1
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2
-
1
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-
1
-
-
-
-
-
-
-
-
-
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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-
-
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1
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723718
Lee
Lysine-21 of Leuconostoc mesen ...
Leuconostoc mesenteroides
Protein Sci.
1
329-334
1992
-
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1
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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
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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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2
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1
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1
-
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-
-
-
-
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-
721573
Crans
Vanadate dimer and tetramer bo ...
Leuconostoc mesenteroides
Biochemistry
29
6698-6706
1990
-
-
-
-
-
-
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
-
-
-
-
-
4
1
-
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-
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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
-
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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1
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
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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
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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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721569
Haghighi
Glucose-6-phosphate dehydrogen ...
Leuconostoc mesenteroides
Biochemistry
21
6421-6428
1982
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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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4
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1
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4
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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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5
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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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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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