BRENDA - Enzyme Database show
show all sequences of 1.2.1.11

Regulation of enzymes of lysine biosynthesis in Corynebacterium glutamicum

Cremer, J.; Treptow, C.; Eggeling, L.; Sahm, H.; J. Gen. Microbiol. 134, 3221-3229 (1988)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
L-isoleucine
inhibits, when added to a final concentration of 10 mM in the assay system produces a decrease of 0.003 units in specific activity
Corynebacterium glutamicum
L-leucine
inhibits, when added to a final concentration of 10 mM in the assay system produces a decrease of 0.004 units in specific activity
Corynebacterium glutamicum
L-lysine
enzyme assayed in the reverse reaction at pH 10
Corynebacterium glutamicum
L-methionine
inhibits, when added to a final concentration of 10 mM in the assay system produces a decrease of 0.004 units in specific activity
Corynebacterium glutamicum
L-threonine
enzyme assayed in the reverse reaction at pH 10
Corynebacterium glutamicum
additional information
-
Corynebacterium glutamicum
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Corynebacterium glutamicum
-
-
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.01
-
grown in minimal medium or in minimal medium plus lysine, methionine and threonine
Corynebacterium glutamicum
0.012
-
grown in minimal medium plus isoleucine
Corynebacterium glutamicum
0.013
-
grown in minimal medium plus lysine or in minimal medium plus threonine
Corynebacterium glutamicum
0.015
-
grown in minimal medium plus leucine or in minimal medium plus methionine
Corynebacterium glutamicum
0.02
-
grown in complex medium
Corynebacterium glutamicum
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-aspartate 4-semialdehyde + phosphate + NADP+
-
390193
Corynebacterium glutamicum
L-4-aspartyl phosphate + NADPH
-
390193
Corynebacterium glutamicum
-
Cofactor
Cofactor
Commentary
Organism
Structure
NADP+
-
Corynebacterium glutamicum
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADP+
-
Corynebacterium glutamicum
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
L-isoleucine
inhibits, when added to a final concentration of 10 mM in the assay system produces a decrease of 0.003 units in specific activity
Corynebacterium glutamicum
L-leucine
inhibits, when added to a final concentration of 10 mM in the assay system produces a decrease of 0.004 units in specific activity
Corynebacterium glutamicum
L-lysine
enzyme assayed in the reverse reaction at pH 10
Corynebacterium glutamicum
L-methionine
inhibits, when added to a final concentration of 10 mM in the assay system produces a decrease of 0.004 units in specific activity
Corynebacterium glutamicum
L-threonine
enzyme assayed in the reverse reaction at pH 10
Corynebacterium glutamicum
additional information
-
Corynebacterium glutamicum
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.01
-
grown in minimal medium or in minimal medium plus lysine, methionine and threonine
Corynebacterium glutamicum
0.012
-
grown in minimal medium plus isoleucine
Corynebacterium glutamicum
0.013
-
grown in minimal medium plus lysine or in minimal medium plus threonine
Corynebacterium glutamicum
0.015
-
grown in minimal medium plus leucine or in minimal medium plus methionine
Corynebacterium glutamicum
0.02
-
grown in complex medium
Corynebacterium glutamicum
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-aspartate 4-semialdehyde + phosphate + NADP+
-
390193
Corynebacterium glutamicum
L-4-aspartyl phosphate + NADPH
-
390193
Corynebacterium glutamicum
-
Other publictions for EC 1.2.1.11
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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9
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6
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1
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1
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2
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1
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6
1
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1
1
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6
6
743196
Subramani
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13
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-
-
-
-
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1
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1
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1
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741535
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Acta Crystallogr. Sect. F
71
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2015
-
1
1
1
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1
2
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5
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1
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2
2
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1
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2
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1
1
2
1
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1
2
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1
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-
2
2
-
-
-
-
1
-
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-
3
3
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742070
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Elaboration of a fragment lib ...
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Bioorg. Med. Chem.
23
6622-6631
2015
-
2
-
-
-
-
65
-
-
-
-
2
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5
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2
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2
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2
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4
63
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2
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4
-
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-
65
63
-
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-
-
2
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-
-
-
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-
-
-
2
-
2
-
-
-
2
-
-
-
-
4
4
-
-
-
742704
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Int. J. Mol. Sci.
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-
-
-
1
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2
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164
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2
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2
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2
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1
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2
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-
2
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-
-
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-
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1
1
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723830
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Structures of ternary complexe ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Acta Crystallogr. Sect. D
68
671-679
2012
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-
1
1
-
-
-
-
-
-
-
2
-
7
-
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1
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-
-
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2
-
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-
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1
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1
1
1
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2
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1
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-
-
-
2
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
724553
Luniwal
Molecular docking and enzymati ...
Streptococcus pneumoniae, Vibrio cholerae
Bioorg. Med. Chem.
20
2950-2956
2012
-
-
2
-
-
-
54
-
-
-
-
2
-
5
-
-
2
-
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2
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2
26
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2
2
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-
54
26
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2
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2
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2
-
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725219
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J. Amino Acids
2011
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2011
-
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8
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6
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7
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12
6
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12
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12
-
8
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6
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12
6
-
-
-
-
-
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6
6
-
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-
725944
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Mol. Biosyst.
7
1564-1575
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-
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1
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4
3
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1
2
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1
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1
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2
1
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1
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1
1
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4
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3
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1
2
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1
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2
1
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2
2
710717
Arachea
Expansion of the aspartate bet ...
Candida albicans
Acta Crystallogr. Sect. D
66
205-212
2010
-
-
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
1
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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726268
Santander
The aspartate-semialdehyde deh ...
Edwardsiella ictaluri, Edwardsiella ictaluri 93-146
PLoS ONE
5
e15944
2010
-
-
-
-
-
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-
-
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2
-
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
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1
1
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684158
Viola
The structure of a redundant e ...
Vibrio cholerae
Acta Crystallogr. Sect. D
D64
321-330
2008
-
1
1
1
-
-
-
-
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1
-
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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1
1
1
1
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1
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1
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2
1
-
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-
1
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-
-
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684192
Vyas
Purification, crystallization ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Acta Crystallogr. Sect. F
64
167-170
2008
-
-
1
1
-
-
-
-
-
-
3
3
-
8
-
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1
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4
2
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1
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4
2
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688468
Singh
Molecular modelling and compar ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
J. Mol. Model.
14
249-263
2008
-
-
-
-
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1
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9
-
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2
2
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1
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1
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1
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2
2
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687340
Cahyanto
Construction of Lactobacillus ...
Lactobacillus plantarum, Lactobacillus plantarum IAM 12477
J. Appl. Microbiol.
102
674-679
2007
-
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1
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2
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3
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1
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2
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670165
Cahyanto
Regulation of aspartokinase, a ...
Lactobacillus plantarum, Lactobacillus plantarum NCIMB 8826
Microbiology
152
105-112
2006
-
1
1
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1
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2
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7
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1
2
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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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2
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1
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1
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674667
Faehnle
Examination of key intermediat ...
Streptococcus pneumoniae
J. Biol. Chem.
281
31031-31040
2006
-
1
1
1
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1
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1
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5
-
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1
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2
1
1
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1
1
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3
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1
1
3
1
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1
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1
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2
1
1
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1
1
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655821
Shafiani
Cloning and characterization o ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
J. Appl. Microbiol.
98
832-838
2005
-
2
1
-
-
-
-
3
-
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1
2
-
9
-
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1
-
-
-
1
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4
1
1
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1
1
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2
-
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2
1
2
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3
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1
2
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1
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1
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4
1
1
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1
1
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-
-
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-
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-
-
673074
Cox
Design, synthesis and analysis ...
Bacteria, Escherichia coli
ChemBiochem
6
2255-2260
2005
-
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1
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3
-
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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
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3
3
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1
3
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3
3
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1
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1
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1
-
-
2
-
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-
-
-
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675355
Faehnle
A new branch in the family: st ...
Methanocaldococcus jannaschii
J. Mol. Biol.
353
1055-1068
2005
-
-
1
1
-
-
2
2
-
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1
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2
-
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1
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-
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2
1
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2
2
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1
2
1
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2
2
2
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1
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1
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2
1
-
-
-
-
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-
-
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675505
Carroll
Petrosamine B, an inhibitor of ...
Helicobacter pylori
J. Nat. Prod.
68
804-806
2005
-
1
1
-
-
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1
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654103
Blanco
The role of substrate-binding ...
Haemophilus influenzae
Acta Crystallogr. Sect. D
60
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2004
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654110
Blanco
Critical catalytic functional ...
Haemophilus influenzae
Acta Crystallogr. Sect. D
60
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2004
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Faehnle
Structural basis for discrimin ...
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Acta Crystallogr. Sect. D
60
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2004
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654891
Alvarez
L-cystine inhibits aspartate-b ...
Escherichia coli
Biochim. Biophys. Acta
1696
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2004
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High-resolution structures rev ...
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2004
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657332
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Cloning, characterization and ...
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2004
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657153
Blanco
Capture of an intermediate in ...
Haemophilus influenzae, no activity in Homo sapiens
Proc. Natl. Acad. Sci. USA
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12613-12617
2003
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Blanco
A structural basis for the mec ...
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Protein Sci.
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390202
Moore
Expression and purification of ...
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Protein Expr. Purif.
25
189-194
2002
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Paris
Overproduction, purification, ...
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Protein Expr. Purif.
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2002
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Expression in Escherichia coli ...
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2000
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Hadfield
Structure of aspartate-beta-se ...
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1999
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Oxyanion specificity of L-Aspa ...
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Inorg. Chem.
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Thomas
Structure of the HOM2 gene of ...
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Cloning and expression of Thio ...
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Cremer
Regulation of enzymes of lysin ...
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Cohen
Aspartate-semialdehyde dehydro ...
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Jagusztyn-Krynicka
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Chatterjee
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Holland
Purification and characterizat ...
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Biochemistry
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Holland
Chemical reactivity at the cat ...
Saccharomyces cerevisiae
Biochemistry
12
2276-2281
1973
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Holland
Adenosine 5-triphosphate induc ...
Saccharomyces cerevisiae
Biochemistry
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Jenkins
Studies of a homoserineless br ...
Neurospora crassa
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2
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2
-
2
1
-
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-
-
-
-
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-
-
-
-
-
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2
-
-
-
-
-
-
-
-
-
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1
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1
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2
-
2
-
2
1
-
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390187
Surdin
Semi-aldehyde aspartic dehydro ...
Saccharomyces cerevisiae
Eur. J. Biochem.
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341-348
1967
1
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5
1
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1
2
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1
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1
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1
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3
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1
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1
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1
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2
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5
1
1
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1
2
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1
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1
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3
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1
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390188
Black
Aspartic beta-semialdehyde deh ...
Saccharomyces cerevisiae
J. Biol. Chem.
213
39-50
1955
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1
4
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1
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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
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4
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1
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1
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1
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3
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3
1
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