BRENDA - Enzyme Database show
show all sequences of 1.17.1.8

NMR studies uncover alternate substrates for dihydrodipicolinate synthase and suggest that dihydrodipicolinate reductase is also a dehydratase

Devenish, S.R.; Blunt, J.W.; Gerrard, J.A.; J. Med. Chem. 53, 4808-4812 (2010)

Data extracted from this reference:

Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Escherichia coli
DHDPR accepts (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid as true substrate rather than dihydrodipicolinate, suggesting that DHDPR catalyzes an overall deoxygenation reaction, likely by a dehydratase-reductase route, substrate specificity, overview. A critical role is played by residue His 159 in the catalytic mechanism of DHDPR. Replacement of this residue with an alanine or a glutamine is reported to result in a 150-200fold reduction in catalytic rate as well as a 6fold increase in KM. His 159 has been proposed to act as a general acid during catalysis, providing the proton required after hydride addition. No activity with beta-hydroxypyruvate and 3-fluoropyruvate
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
DHDPR accepts (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid as true substrate rather than dihydrodipicolinate, suggesting that DHDPR catalyzes an overall deoxygenation reaction, likely by a dehydratase-reductase route, substrate specificity, overview. A critical role is played by residue His 159 in the catalytic mechanism of DHDPR. Replacement of this residue with an alanine or a glutamine is reported to result in a 150-200fold reduction in catalytic rate as well as a 6fold increase in KM. His 159 has been proposed to act as a general acid during catalysis, providing the proton required after hydride addition. No activity with beta-hydroxypyruvate and 3-fluoropyruvate
712704
Escherichia coli
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
More
crystal structure modelling and analysis, PDB ID 1ARZ, overview
Escherichia coli
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
dehydration assay at
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Escherichia coli
DHDPR accepts (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid as true substrate rather than dihydrodipicolinate, suggesting that DHDPR catalyzes an overall deoxygenation reaction, likely by a dehydratase-reductase route, substrate specificity, overview. A critical role is played by residue His 159 in the catalytic mechanism of DHDPR. Replacement of this residue with an alanine or a glutamine is reported to result in a 150-200fold reduction in catalytic rate as well as a 6fold increase in KM. His 159 has been proposed to act as a general acid during catalysis, providing the proton required after hydride addition. No activity with beta-hydroxypyruvate and 3-fluoropyruvate
?
-
-
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
DHDPR accepts (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid as true substrate rather than dihydrodipicolinate, suggesting that DHDPR catalyzes an overall deoxygenation reaction, likely by a dehydratase-reductase route, substrate specificity, overview. A critical role is played by residue His 159 in the catalytic mechanism of DHDPR. Replacement of this residue with an alanine or a glutamine is reported to result in a 150-200fold reduction in catalytic rate as well as a 6fold increase in KM. His 159 has been proposed to act as a general acid during catalysis, providing the proton required after hydride addition. No activity with beta-hydroxypyruvate and 3-fluoropyruvate
712704
Escherichia coli
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
More
crystal structure modelling and analysis, PDB ID 1ARZ, overview
Escherichia coli
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
dehydration assay at
Escherichia coli
General Information
General Information
Commentary
Organism
metabolism
DHDPR is central to the diaminopimelate pathway for lysine biosynthesis
Escherichia coli
additional information
NMR studies uncover that dihydrodipicolinate reductase is also a dehydratase, overview
Escherichia coli
General Information (protein specific)
General Information
Commentary
Organism
metabolism
DHDPR is central to the diaminopimelate pathway for lysine biosynthesis
Escherichia coli
additional information
NMR studies uncover that dihydrodipicolinate reductase is also a dehydratase, overview
Escherichia coli
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)
744277
Watkin
Plant DHDPR forms a dimer wit ...
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475
137-150
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-
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1
3
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4
12
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-
3
4
-
6
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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
-
-
3
4
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-
-
-
11
4
4
-
-
6
4
-
-
-
-
3
3
-
-
-
746555
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Brucella abortus phosphoglyce ...
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1
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6
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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
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743963
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72
885-891
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1
1
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2
2
-
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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-
-
-
-
-
-
1
1
-
-
-
745538
Sagong
Structural insight into dihyd ...
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J. Microbiol. Biotechnol.
26
226-232
2016
-
-
1
1
-
-
-
-
-
-
-
4
-
4
-
-
1
1
-
-
-
-
10
1
-
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-
-
-
-
-
2
-
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-
1
2
1
-
-
-
-
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4
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1
-
-
-
-
10
1
-
-
-
-
-
-
-
-
-
1
1
-
-
-
746195
Trigoso
Cloning, expression, and puri ...
Escherichia coli
PLoS ONE
11
e0146525
2016
-
-
1
1
-
-
-
1
-
-
1
1
-
5
-
-
1
-
-
-
-
-
3
1
-
-
-
-
-
-
-
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
-
-
-
-
-
-
-
-
-
-
-
-
-
-
746457
Shrivastava
Inhibition of Mycobacterium t ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Sci. Rep.
6
30827
2016
-
-
1
-
-
-
-
-
-
-
-
-
-
5
-
-
-
-
-
-
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2
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1
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2
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746463
Christensen
Structure and function of cya ...
Trichormus variabilis
Sci. Rep.
6
37111
2016
-
-
1
1
-
-
1
2
-
-
1
-
-
7
-
-
-
-
-
-
-
-
1
1
1
-
-
-
-
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-
-
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-
1
-
1
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1
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2
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1
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-
1
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
726634
Kaushik
Cloning, expression, crystalli ...
Acinetobacter baumannii
Acta Crystallogr. Sect. F
69
653-656
2013
-
-
1
1
-
-
-
-
-
-
-
-
-
3
-
-
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1
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1
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723702
Dogovski
Comparative structure and func ...
Staphylococcus aureus, Staphylococcus aureus MRSA
Protein Expr. Purif.
85
66-76
2012
-
-
1
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-
-
-
4
-
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1
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-
7
-
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1
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-
1
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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
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-
1
4
-
-
-
-
-
1
1
-
-
-
721427
Dommaraju
Catalytic mechanism and cofact ...
Staphylococcus aureus, Staphylococcus aureus MRSA
Arch. Biochem. Biophys.
512
167-174
2011
-
-
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
Structure and nucleotide speci ...
Staphylococcus aureus, Staphylococcus aureus COL
FEBS Lett.
585
2561-2567
2011
-
-
1
1
1
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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 ...
Pseudomonas aeruginosa
Int. J. Integr. Biol.
11
145-152
2011
-
-
1
-
-
-
-
2
-
-
3
-
-
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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1
2
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2
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3
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1
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2
1
1
1
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-
1
1
-
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712704
Devenish
NMR studies uncover alternate ...
Escherichia coli
J. Med. Chem.
53
4808-4812
2010
-
-
-
-
-
-
-
-
-
-
-
1
-
1
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1
1
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1
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1
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-
1
1
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-
-
1
-
-
-
-
2
2
-
-
-
721156
Janowski
The structure of dihydrodipico ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Acta Crystallogr. Sect. D
66
61-72
2010
-
-
1
1
-
-
-
2
-
-
-
-
-
5
-
-
1
-
-
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4
1
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2
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1
2
1
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2
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1
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-
4
1
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-
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-
1
1
-
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-
710760
Dommaraju
Cloning, expression and crysta ...
Staphylococcus aureus, Staphylococcus aureus MRSA252
Acta Crystallogr. Sect. F
66
57-60
2009
-
-
1
1
-
-
-
-
-
-
1
-
-
4
-
-
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
1
-
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-
687457
Pearce
Characterization of dihydrodip ...
Thermotoga maritima, Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
J. Biochem.
143
617-623
2008
-
-
1
-
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-
2
6
-
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-
5
-
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1
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1
1
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1
6
-
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2
2
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1
2
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2
2
6
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1
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1
1
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1
6
-
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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
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2
2
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2
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1
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3
1
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2
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1
1
2
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2
2
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1
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3
1
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1
1
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-
689539
Shimizu
Dihydrodipicolinate reductase- ...
Arabidopsis thaliana
Plant J.
52
539-547
2007
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-
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4
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1
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3
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2
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4
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670165
Cahyanto
Regulation of aspartokinase, a ...
Lactobacillus plantarum
Microbiology
152
105-112
2006
-
-
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-
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1
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3
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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
-
-
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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1
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1
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1
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1
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-
654674
Cirilli
The three-dimensional structur ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Biochemistry
42
10644-10650
2003
-
-
1
1
2
-
1
6
-
-
-
1
-
5
-
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-
1
-
-
1
-
2
1
-
-
-
-
-
-
-
2
-
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1
2
1
2
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1
-
6
-
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1
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1
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2
1
-
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-
390623
Paiva
Inhibitors of dihydrodipicolin ...
Escherichia coli, Mycobacterium tuberculosis
Biochim. Biophys. Acta
1545
67-77
2001
-
2
2
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-
4
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2
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3
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2
1
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3
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3
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2
2
3
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4
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2
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2
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3
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390622
Garcia-Rodriguez
Characterization of the Sinorh ...
Sinorhizobium meliloti
Arch. Microbiol.
173
438-444
2000
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4
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390620
Coulter
-
Escherichia coli dihydrodipico ...
Escherichia coli
Pestic. Sci.
55
887-895
1999
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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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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
-
Regulation of the enzymes of l ...
Lysinibacillus sphaericus
J. Gen. Microbiol.
132
3169-3177
1986
-
-
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3
-
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2
-
1
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390610
Rao
Regulation of lysine and dipic ...
Brevibacillus brevis
Arch. Microbiol.
141
143-150
1985
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2
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390611
Bouvier
Nucleotide sequence and expres ...
Escherichia coli
J. Biol. Chem.
259
14829-14834
1984
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1
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2
1
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2
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390612
Tyagi
Partial purification and chara ...
Zea mays
Plant Physiol.
73
687-691
1983
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7
2
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3
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390613
Tosaka
-
Pathway and regulation of lysi ...
Corynebacterium glutamicum
Agric. Biol. Chem.
42
95-100
1978
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390614
Kimura
Dihydrodipicolinate reductases ...
Bacillus cereus, Bacillus megaterium
J. Biochem.
81
1367-1373
1977
2
-
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8
4
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2
2
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2
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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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-
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-
6
-
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2
2
-
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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1
2
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-
2
-
6
-
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390617
Tamir
Dihydrodipicolinic acid reduct ...
Escherichia coli
J. Biol. Chem.
249
3034-3040
1974
1
-
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-
-
7
1
-
-
1
1
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-
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390618
Tamir
-
Dihydrodipicolinic acid reduct ...
Escherichia coli
Methods Enzymol.
17B
134-139
1971
1
-
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-
3
1
-
-
1
1
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-
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-
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-
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-
-
390619
Farkas
The reduction step in diaminop ...
Escherichia coli
J. Biol. Chem.
240
4717-4722
1965
-
-
-
-
-
-
-
-
-
-
-
1
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