BRENDA - Enzyme Database show
show all sequences of 1.17.1.8

Characterization of dihydrodipicolinate reductase from Thermotoga maritima reveals evolution of substrate binding kinetics

Pearce, F.G.; Sprissler, C.; Gerrard, J.A.; J. Biochem. 143, 617-623 (2008)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expressed in Escherichia coli XL-1 Blue cells
Thermotoga maritima
Inhibitors
Inhibitors
Commentary
Organism
Structure
2,3-dihydrodipicolinate
the enzyme is inhibited by high concentrations of 2,3-dihydrodipicolinate
Thermotoga maritima
NADH
-
Thermotoga maritima
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0006
-
NADPH
apparent value, at 30°C
Thermotoga maritima
0.0018
-
NADH
apparent value, at 45°C
Thermotoga maritima
0.0021
-
NADPH
apparent value, at 45°C
Thermotoga maritima
0.0025
-
NADH
apparent value, at 30°C
Thermotoga maritima
0.0076
-
2,3-dihydrodipicolinate
apparent value, at 30°C
Thermotoga maritima
0.013
-
2,3-dihydrodipicolinate
apparent value, at 45°C
Thermotoga maritima
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Thermotoga maritima
Q9X1K8
-
-
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
Q9X1K8
-
-
Purification (Commentary)
Commentary
Organism
His-Trap column chromatography
Thermotoga maritima
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2,3-dihydrodipicolinate + NAD(P)H
-
687457
Thermotoga maritima
2,3,4,5-tetrahydrodipicolinate + NAD(P)+
-
-
-
?
Subunits
Subunits
Commentary
Organism
tetramer
x-ray crystallography
Thermotoga maritima
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
80
95
the enzyme is stable for up to 48 h at 80°C, the melting temperature of DHDPR is at 95.7°C
Thermotoga maritima
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.093
-
NADH
apparent value, at 30°C
Thermotoga maritima
0.49
-
NADH
apparent value, at 45°C
Thermotoga maritima
2.6
-
NADPH
apparent value, at 30°C
Thermotoga maritima
8.1
-
2,3-dihydrodipicolinate
apparent value, at 30°C
Thermotoga maritima
17
-
NADPH
apparent value, at 45°C
Thermotoga maritima
19
-
2,3-dihydrodipicolinate
apparent value, at 45°C
Thermotoga maritima
Cofactor
Cofactor
Commentary
Organism
Structure
NADH
the enzyme has a greater affinity for NADPH than for NADH
Thermotoga maritima
NADPH
the enzyme has a greater affinity for NADPH than for NADH
Thermotoga maritima
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.0051
-
NADH
at 30°C
Thermotoga maritima
0.0081
-
NADH
at 45°C
Thermotoga maritima
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli XL-1 Blue cells
Thermotoga maritima
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADH
the enzyme has a greater affinity for NADPH than for NADH
Thermotoga maritima
NADPH
the enzyme has a greater affinity for NADPH than for NADH
Thermotoga maritima
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
2,3-dihydrodipicolinate
the enzyme is inhibited by high concentrations of 2,3-dihydrodipicolinate
Thermotoga maritima
NADH
-
Thermotoga maritima
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.0051
-
NADH
at 30°C
Thermotoga maritima
0.0081
-
NADH
at 45°C
Thermotoga maritima
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0006
-
NADPH
apparent value, at 30°C
Thermotoga maritima
0.0018
-
NADH
apparent value, at 45°C
Thermotoga maritima
0.0021
-
NADPH
apparent value, at 45°C
Thermotoga maritima
0.0025
-
NADH
apparent value, at 30°C
Thermotoga maritima
0.0076
-
2,3-dihydrodipicolinate
apparent value, at 30°C
Thermotoga maritima
0.013
-
2,3-dihydrodipicolinate
apparent value, at 45°C
Thermotoga maritima
Purification (Commentary) (protein specific)
Commentary
Organism
His-Trap column chromatography
Thermotoga maritima
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2,3-dihydrodipicolinate + NAD(P)H
-
687457
Thermotoga maritima
2,3,4,5-tetrahydrodipicolinate + NAD(P)+
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
tetramer
x-ray crystallography
Thermotoga maritima
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
80
95
the enzyme is stable for up to 48 h at 80°C, the melting temperature of DHDPR is at 95.7°C
Thermotoga maritima
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.093
-
NADH
apparent value, at 30°C
Thermotoga maritima
0.49
-
NADH
apparent value, at 45°C
Thermotoga maritima
2.6
-
NADPH
apparent value, at 30°C
Thermotoga maritima
8.1
-
2,3-dihydrodipicolinate
apparent value, at 30°C
Thermotoga maritima
17
-
NADPH
apparent value, at 45°C
Thermotoga maritima
19
-
2,3-dihydrodipicolinate
apparent value, at 45°C
Thermotoga maritima
Other publictions for EC 1.17.1.8
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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11
4
4
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6
4
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4
5
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1
4
3
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-
4
5
12
-
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3
4
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1
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2
2
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5
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1
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2
1
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1
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1
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2
2
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1
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2
1
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-
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-
-
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4
-
4
-
-
1
1
-
-
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10
1
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2
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1
2
1
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4
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1
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-
10
1
-
-
-
-
-
-
-
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1
1
-
-
-
746195
Trigoso
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11
e0146525
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1
1
-
-
-
1
-
-
1
1
-
5
-
-
1
-
-
-
-
-
3
1
-
-
-
-
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-
-
2
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1
2
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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746457
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1
-
-
-
-
-
-
-
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5
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2
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2
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746463
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Structure and function of cya ...
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-
1
1
-
-
1
2
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-
1
-
-
7
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1
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
1
1
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726634
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Acta Crystallogr. Sect. F
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-
1
1
-
-
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-
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3
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85
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-
1
-
-
-
-
4
-
-
1
-
-
7
-
-
1
-
-
-
1
-
4
1
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1
4
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2
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1
2
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4
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1
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1
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1
-
4
1
-
-
1
4
-
-
-
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-
1
1
-
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721427
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-
-
1
-
-
-
1
4
-
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7
-
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4
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2
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1
2
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1
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4
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4
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722272
Girish
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585
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-
-
1
1
1
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-
-
-
-
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-
3
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1
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4
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2
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1
2
1
1
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1
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4
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722411
Anand
-
Molecular cloning, biochemical ...
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2011
-
-
1
-
-
-
-
2
-
-
3
-
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1
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1
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2
1
1
1
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1
1
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2
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2
1
1
1
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1
1
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712704
Devenish
NMR studies uncover alternate ...
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53
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2010
-
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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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2
2
-
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-
721156
Janowski
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Acta Crystallogr. Sect. D
66
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2010
-
-
1
1
-
-
-
2
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5
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1
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4
1
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1
2
1
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1
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4
1
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1
1
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710760
Dommaraju
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Acta Crystallogr. Sect. F
66
57-60
2009
-
-
1
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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1
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1
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1
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1
1
-
-
-
687457
Pearce
Characterization of dihydrodip ...
Thermotoga maritima, Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
J. Biochem.
143
617-623
2008
-
-
1
-
-
-
2
6
-
-
-
-
-
5
-
-
1
-
-
-
-
-
1
1
-
-
1
6
-
-
-
2
2
-
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-
1
2
-
-
-
-
2
2
6
-
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1
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-
1
1
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1
6
-
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-
-
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-
696300
Ge
Binding synergy and cooperativ ...
Escherichia coli
Biochemistry
47
9966-9980
2008
2
1
1
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-
-
2
-
-
-
2
2
-
2
-
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1
-
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-
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3
1
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2
-
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2
1
1
2
-
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-
-
2
-
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-
-
2
2
-
-
-
1
-
-
-
-
3
1
-
-
-
-
-
-
-
-
-
1
1
-
-
-
689539
Shimizu
Dihydrodipicolinate reductase- ...
Arabidopsis thaliana
Plant J.
52
539-547
2007
-
-
-
-
-
-
-
-
4
-
1
-
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3
-
-
-
-
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2
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4
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1
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2
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670165
Cahyanto
Regulation of aspartokinase, a ...
Lactobacillus plantarum
Microbiology
152
105-112
2006
-
-
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1
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3
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1
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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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-
677262
Cahyanto
Cloning of Lactobacillus plant ...
Lactobacillus plantarum, Lactobacillus plantarum IAM 12477
World J. Microbiol. Biotechnol.
22
409-416
2006
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654674
Cirilli
The three-dimensional structur ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Biochemistry
42
10644-10650
2003
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6
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390623
Paiva
Inhibitors of dihydrodipicolin ...
Escherichia coli, Mycobacterium tuberculosis
Biochim. Biophys. Acta
1545
67-77
2001
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2
2
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390622
Garcia-Rodriguez
Characterization of the Sinorh ...
Sinorhizobium meliloti
Arch. Microbiol.
173
438-444
2000
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390620
Coulter
-
Escherichia coli dihydrodipico ...
Escherichia coli
Pestic. Sci.
55
887-895
1999
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3
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390625
Scapin
Three-dimensional structure of ...
Escherichia coli
Biochemistry
36
15081-15088
1997
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390621
Reddy
Interaction of pyridine nucleo ...
Escherichia coli
Biochemistry
35
13294-13302
1996
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390624
Reddy
Expression, purification, and ...
Escherichia coli
Biochemistry
34
3492-3501
1995
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1
1
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8
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390626
Scapin
Three-dimensional structure of ...
Escherichia coli
Biochemistry
34
3502-3512
1995
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390608
Cremer
-
Cloning the dapA dapB cluster ...
Corynebacterium glutamicum
Mol. Gen. Genet.
220
478-480
1990
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390194
Bartlett
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Regulation of the enzymes of l ...
Lysinibacillus sphaericus
J. Gen. Microbiol.
132
3169-3177
1986
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390610
Rao
Regulation of lysine and dipic ...
Brevibacillus brevis
Arch. Microbiol.
141
143-150
1985
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390611
Bouvier
Nucleotide sequence and expres ...
Escherichia coli
J. Biol. Chem.
259
14829-14834
1984
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390612
Tyagi
Partial purification and chara ...
Zea mays
Plant Physiol.
73
687-691
1983
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2
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390613
Tosaka
-
Pathway and regulation of lysi ...
Corynebacterium glutamicum
Agric. Biol. Chem.
42
95-100
1978
2
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390614
Kimura
Dihydrodipicolinate reductases ...
Bacillus cereus, Bacillus megaterium
J. Biochem.
81
1367-1373
1977
2
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4
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390615
Kimura
A new flavin enzyme catalyzing ...
Bacillus subtilis, Bacillus subtilis PCI 219
J. Biochem.
77
405-413
1975
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6
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390616
Kimura
A new flavin enzyme catalyzing ...
Bacillus subtilis, Bacillus subtilis PCI 219
J. Biochem.
77
415-420
1975
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390617
Tamir
Dihydrodipicolinic acid reduct ...
Escherichia coli
J. Biol. Chem.
249
3034-3040
1974
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390618
Tamir
-
Dihydrodipicolinic acid reduct ...
Escherichia coli
Methods Enzymol.
17B
134-139
1971
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390619
Farkas
The reduction step in diaminop ...
Escherichia coli
J. Biol. Chem.
240
4717-4722
1965
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