BRENDA - Enzyme Database
show all sequences of 1.1.1.282

Site-directed mutagenesis of the active site region in the quinate/shikimate 5-dehydrogenase YdiB of Escherichia coli

Lindner, H.A.; Nadeau, G.; Matte, A.; Michel, G.; Menard, R.; Cygler, M.; J. Biol. Chem. 280, 7162-7169 (2005)

Data extracted from this reference:

Application
Application
Commentary
Organism
agriculture
development of novel herbicides
Escherichia coli
medicine
development of novel antimicrobial agents
Escherichia coli
Engineering
Protein Variants
Commentary
Organism
D107A
site-directed mutagenesis
Escherichia coli
K71G
site-directed mutagenesis
Escherichia coli
N92A
site-directed mutagenesis
Escherichia coli
Q262A
site-directed mutagenesis
Escherichia coli
S22A
site-directed mutagenesis
Escherichia coli
S67A
site-directed mutagenesis, increased activity compared to wild type enzyme
Escherichia coli
T106A
site-directed mutagenesis
Escherichia coli
Y39F
site-directed mutagenesis
Escherichia coli
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0004
-
NAD+
mutant K71A, in the presence of shikimate, 20C, pH 9.0
Escherichia coli
0.0017
-
shikimate
mutant S67A, 20C, pH 9.0
Escherichia coli
0.002
-
NAD+
mutant K71A, in the presence of L-quinate, 20C, pH 9.0
Escherichia coli
0.0028
-
shikimate
mutant Q262A, 20C, pH 9.0
Escherichia coli
0.0029
-
shikimate
wild type enzyme, 20C, pH 9.0
Escherichia coli
0.0032
-
shikimate
mutant S22A, 20C, pH 9.0
Escherichia coli
0.0032
-
shikimate
mutant Y39F, 20C, pH 9.0
Escherichia coli
0.0054
-
L-quinate
mutant Y39F, 20C, pH 9.0
Escherichia coli
0.0057
-
L-quinate
mutant S22A, 20C, pH 9.0
Escherichia coli
0.0068
-
NAD+
mutant D107A, in the presence of shikimate, 20C, pH 9.0
Escherichia coli
0.0091
-
L-quinate
wild type enzyme, 20C, pH 9.0
Escherichia coli
0.0107
-
NAD+
mutant Q262A, in the presence of shikimate, 20C, pH 9.0
Escherichia coli
0.0121
-
NAD+
mutant S67A, in the presence of L-quinate, 20C, pH 9.0
Escherichia coli
0.0122
-
NAD+
wild type enzyme, in the presence of shikimate, 20C, pH 9.0
Escherichia coli
0.0125
-
NAD+
mutant Y39F, in the presence of L-quinate, 20C, pH 9.0
Escherichia coli
0.0126
-
NAD+
mutant S67A, in the presence of shikimate, 20C, pH 9.0
Escherichia coli
0.0136
-
L-quinate
mutant Q262A, 20C, pH 9.0
Escherichia coli
0.0142
-
NAD+
mutant Q262A, in the presence of L-quinate, 20C, pH 9.0
Escherichia coli
0.0157
-
L-quinate
mutant S67A, 20C, pH 9.0
Escherichia coli
0.0158
-
NAD+
mutant T106A, in the presence of shihikimat, 20C, pH 9.0
Escherichia coli
0.0158
-
NAD+
mutant Y39F, in the presence of shikimate, 20C, pH 9.0
Escherichia coli
0.0168
-
NAD+
mutant S22A, in the presence of L-quinate, 20C, pH 9.0
Escherichia coli
0.018
-
NAD+
mutant S22A, in the presence of shikimate, 20C, pH 9.0
Escherichia coli
0.0184
-
NAD+
wild type enzyme, in the presence of L-quinate, 20C, pH 9.0
Escherichia coli
0.0578
-
NAD+
mutant T106A, in the presence of L-quinate, 20C, pH 9.0
Escherichia coli
0.199
-
shikimate
mutant T106A, 20C, pH 9.0
Escherichia coli
0.513
-
shikimate
mutant K71A, 20C, pH 9.0
Escherichia coli
20.52
-
L-quinate
mutant T106A, 20C, pH 9.0
Escherichia coli
32.68
-
L-quinate
mutant K71A, 20C, pH 9.0
Escherichia coli
40.07
-
shikimate
mutant D107A, 20C, pH 9.0
Escherichia coli
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
31350
-
2 * 31350, wild type enzyme, gel filtration
Escherichia coli
33000
-
SDS-PAGE, mutant N92A
Escherichia coli
57000
-
SDS-PAGE, wild type enzyme
Escherichia coli
Organism
Organism
UniProt
Commentary
Textmining
Escherichia coli
P0A6D5
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
3-dehydroquinate + NADPH + H+
-
656292
Escherichia coli
L-quinate + NADP+
-
-
-
r
3-dehydroshikimate + NADH + H+
-
656292
Escherichia coli
shikimate + NAD+
-
-
-
r
L-quinate + NADP+
-
656292
Escherichia coli
3-dehydroquinate + NADPH + H+
-
-
-
r
shikimate + NAD+
-
656292
Escherichia coli
3-dehydroshikimate + NADH + H+
-
-
-
r
Subunits
Subunits
Commentary
Organism
dimer
2 * 31350, wild type enzyme, gel filtration
Escherichia coli
Synonyms
Synonyms
Commentary
Organism
quinate/shikimate 5-dehydrogenase
-
Escherichia coli
YdiB
-
Escherichia coli
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.004
-
NAD+
mutant K71A, in the presence of L-quinate, 20C, pH 9.0
Escherichia coli
0.011
-
shikimate
mutant K71A, 20C, pH 9.0
Escherichia coli
0.012
-
L-quinate
mutant K71A, 20C, pH 9.0
Escherichia coli
0.012
-
NAD+
mutant K71A, in the presence of shikimate, 20C, pH 9.0
Escherichia coli
0.022
-
NAD+
mutant D107A, in the presence of shikimate, 20C, pH 9.0
Escherichia coli
0.022
-
NAD+
mutant Q262A, in the presence of shikimate, 20C, pH 9.0
Escherichia coli
0.023
-
NAD+
mutant S67A, in the presence of L-quinate, 20C, pH 9.0
Escherichia coli
0.024
-
L-quinate
mutant S67A, 20C, pH 9.0
Escherichia coli
0.043
-
NAD+
mutant Q262A, in the presence of L-quinate, 20C, pH 9.0
Escherichia coli
0.05
-
shikimate
mutant Q262A, 20C, pH 9.0
Escherichia coli
0.05
-
L-quinate
mutant Q262A, 20C, pH 9.0
Escherichia coli
0.054
-
shikimate
mutant T106A, 20C, pH 9.0
Escherichia coli
0.06
-
L-quinate
mutant Y39F, 20C, pH 9.0
Escherichia coli
0.068
-
L-quinate
mutant S22A, 20C, pH 9.0
Escherichia coli
0.082
-
NAD+
mutant S22A, in the presence of L-quinate, 20C, pH 9.0
Escherichia coli
0.09
-
NAD+
mutant Y39F, in the presence of L-quinate, 20C, pH 9.0
Escherichia coli
0.091
-
shikimate
wild type enzyme, 20C, pH 9.0
Escherichia coli
0.105
-
NAD+
wild type enzyme, in the presence of shikimate, 20C, pH 9.0
Escherichia coli
0.108
-
NAD+
mutant T106A, in the presence of shihikimat, 20C, pH 9.0
Escherichia coli
0.109
-
shikimate
mutant S22A, 20C, pH 9.0
Escherichia coli
0.113
-
L-quinate
wild type enzyme, 20C, pH 9.0
Escherichia coli
0.122
-
NAD+
mutant T106A, in the presence of L-quinate, 20C, pH 9.0
Escherichia coli
0.132
-
shikimate
mutant D107A, 20C, pH 9.0
Escherichia coli
0.142
-
NAD+
wild type enzyme, in the presence of L-quinate, 20C, pH 9.0
Escherichia coli
0.148
-
shikimate
mutant S67A, 20C, pH 9.0
Escherichia coli
0.153
-
NAD+
mutant S22A, in the presence of shikimate, 20C, pH 9.0
Escherichia coli
0.178
-
NAD+
mutant S67A, in the presence of shikimate, 20C, pH 9.0
Escherichia coli
0.187
-
shikimate
mutant Y39F, 20C, pH 9.0
Escherichia coli
0.233
-
L-quinate
mutant T106A, 20C, pH 9.0
Escherichia coli
0.24
-
NAD+
mutant Y39F, in the presence of shikimate, 20C, pH 9.0
Escherichia coli
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
-
Escherichia coli
NADH
-
Escherichia coli
NADP+
-
Escherichia coli
NADPH
-
Escherichia coli
Application (protein specific)
Application
Commentary
Organism
agriculture
development of novel herbicides
Escherichia coli
medicine
development of novel antimicrobial agents
Escherichia coli
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
-
Escherichia coli
NADH
-
Escherichia coli
NADP+
-
Escherichia coli
NADPH
-
Escherichia coli
Engineering (protein specific)
Protein Variants
Commentary
Organism
D107A
site-directed mutagenesis
Escherichia coli
K71G
site-directed mutagenesis
Escherichia coli
N92A
site-directed mutagenesis
Escherichia coli
Q262A
site-directed mutagenesis
Escherichia coli
S22A
site-directed mutagenesis
Escherichia coli
S67A
site-directed mutagenesis, increased activity compared to wild type enzyme
Escherichia coli
T106A
site-directed mutagenesis
Escherichia coli
Y39F
site-directed mutagenesis
Escherichia coli
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0004
-
NAD+
mutant K71A, in the presence of shikimate, 20C, pH 9.0
Escherichia coli
0.0017
-
shikimate
mutant S67A, 20C, pH 9.0
Escherichia coli
0.002
-
NAD+
mutant K71A, in the presence of L-quinate, 20C, pH 9.0
Escherichia coli
0.0028
-
shikimate
mutant Q262A, 20C, pH 9.0
Escherichia coli
0.0029
-
shikimate
wild type enzyme, 20C, pH 9.0
Escherichia coli
0.0032
-
shikimate
mutant S22A, 20C, pH 9.0
Escherichia coli
0.0032
-
shikimate
mutant Y39F, 20C, pH 9.0
Escherichia coli
0.0054
-
L-quinate
mutant Y39F, 20C, pH 9.0
Escherichia coli
0.0057
-
L-quinate
mutant S22A, 20C, pH 9.0
Escherichia coli
0.0068
-
NAD+
mutant D107A, in the presence of shikimate, 20C, pH 9.0
Escherichia coli
0.0091
-
L-quinate
wild type enzyme, 20C, pH 9.0
Escherichia coli
0.0107
-
NAD+
mutant Q262A, in the presence of shikimate, 20C, pH 9.0
Escherichia coli
0.0121
-
NAD+
mutant S67A, in the presence of L-quinate, 20C, pH 9.0
Escherichia coli
0.0122
-
NAD+
wild type enzyme, in the presence of shikimate, 20C, pH 9.0
Escherichia coli
0.0125
-
NAD+
mutant Y39F, in the presence of L-quinate, 20C, pH 9.0
Escherichia coli
0.0126
-
NAD+
mutant S67A, in the presence of shikimate, 20C, pH 9.0
Escherichia coli
0.0136
-
L-quinate
mutant Q262A, 20C, pH 9.0
Escherichia coli
0.0142
-
NAD+
mutant Q262A, in the presence of L-quinate, 20C, pH 9.0
Escherichia coli
0.0157
-
L-quinate
mutant S67A, 20C, pH 9.0
Escherichia coli
0.0158
-
NAD+
mutant T106A, in the presence of shihikimat, 20C, pH 9.0
Escherichia coli
0.0158
-
NAD+
mutant Y39F, in the presence of shikimate, 20C, pH 9.0
Escherichia coli
0.0168
-
NAD+
mutant S22A, in the presence of L-quinate, 20C, pH 9.0
Escherichia coli
0.018
-
NAD+
mutant S22A, in the presence of shikimate, 20C, pH 9.0
Escherichia coli
0.0184
-
NAD+
wild type enzyme, in the presence of L-quinate, 20C, pH 9.0
Escherichia coli
0.0578
-
NAD+
mutant T106A, in the presence of L-quinate, 20C, pH 9.0
Escherichia coli
0.199
-
shikimate
mutant T106A, 20C, pH 9.0
Escherichia coli
0.513
-
shikimate
mutant K71A, 20C, pH 9.0
Escherichia coli
20.52
-
L-quinate
mutant T106A, 20C, pH 9.0
Escherichia coli
32.68
-
L-quinate
mutant K71A, 20C, pH 9.0
Escherichia coli
40.07
-
shikimate
mutant D107A, 20C, pH 9.0
Escherichia coli
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
31350
-
2 * 31350, wild type enzyme, gel filtration
Escherichia coli
33000
-
SDS-PAGE, mutant N92A
Escherichia coli
57000
-
SDS-PAGE, wild type enzyme
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
3-dehydroquinate + NADPH + H+
-
656292
Escherichia coli
L-quinate + NADP+
-
-
-
r
3-dehydroshikimate + NADH + H+
-
656292
Escherichia coli
shikimate + NAD+
-
-
-
r
L-quinate + NADP+
-
656292
Escherichia coli
3-dehydroquinate + NADPH + H+
-
-
-
r
shikimate + NAD+
-
656292
Escherichia coli
3-dehydroshikimate + NADH + H+
-
-
-
r
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
2 * 31350, wild type enzyme, gel filtration
Escherichia coli
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.004
-
NAD+
mutant K71A, in the presence of L-quinate, 20C, pH 9.0
Escherichia coli
0.011
-
shikimate
mutant K71A, 20C, pH 9.0
Escherichia coli
0.012
-
L-quinate
mutant K71A, 20C, pH 9.0
Escherichia coli
0.012
-
NAD+
mutant K71A, in the presence of shikimate, 20C, pH 9.0
Escherichia coli
0.022
-
NAD+
mutant D107A, in the presence of shikimate, 20C, pH 9.0
Escherichia coli
0.022
-
NAD+
mutant Q262A, in the presence of shikimate, 20C, pH 9.0
Escherichia coli
0.023
-
NAD+
mutant S67A, in the presence of L-quinate, 20C, pH 9.0
Escherichia coli
0.024
-
L-quinate
mutant S67A, 20C, pH 9.0
Escherichia coli
0.043
-
NAD+
mutant Q262A, in the presence of L-quinate, 20C, pH 9.0
Escherichia coli
0.05
-
shikimate
mutant Q262A, 20C, pH 9.0
Escherichia coli
0.05
-
L-quinate
mutant Q262A, 20C, pH 9.0
Escherichia coli
0.054
-
shikimate
mutant T106A, 20C, pH 9.0
Escherichia coli
0.06
-
L-quinate
mutant Y39F, 20C, pH 9.0
Escherichia coli
0.068
-
L-quinate
mutant S22A, 20C, pH 9.0
Escherichia coli
0.082
-
NAD+
mutant S22A, in the presence of L-quinate, 20C, pH 9.0
Escherichia coli
0.09
-
NAD+
mutant Y39F, in the presence of L-quinate, 20C, pH 9.0
Escherichia coli
0.091
-
shikimate
wild type enzyme, 20C, pH 9.0
Escherichia coli
0.105
-
NAD+
wild type enzyme, in the presence of shikimate, 20C, pH 9.0
Escherichia coli
0.108
-
NAD+
mutant T106A, in the presence of shihikimat, 20C, pH 9.0
Escherichia coli
0.109
-
shikimate
mutant S22A, 20C, pH 9.0
Escherichia coli
0.113
-
L-quinate
wild type enzyme, 20C, pH 9.0
Escherichia coli
0.122
-
NAD+
mutant T106A, in the presence of L-quinate, 20C, pH 9.0
Escherichia coli
0.132
-
shikimate
mutant D107A, 20C, pH 9.0
Escherichia coli
0.142
-
NAD+
wild type enzyme, in the presence of L-quinate, 20C, pH 9.0
Escherichia coli
0.148
-
shikimate
mutant S67A, 20C, pH 9.0
Escherichia coli
0.153
-
NAD+
mutant S22A, in the presence of shikimate, 20C, pH 9.0
Escherichia coli
0.178
-
NAD+
mutant S67A, in the presence of shikimate, 20C, pH 9.0
Escherichia coli
0.187
-
shikimate
mutant Y39F, 20C, pH 9.0
Escherichia coli
0.233
-
L-quinate
mutant T106A, 20C, pH 9.0
Escherichia coli
0.24
-
NAD+
mutant Y39F, in the presence of shikimate, 20C, pH 9.0
Escherichia coli
Other publictions for EC 1.1.1.282
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
Synonyms
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)
740881
Garcia
The role of the ydiB gene, whi ...
Escherichia coli, Escherichia coli JM101
J. Mol. Microbiol. Biotechnol.
27
11-21
2016
-
1
1
-
1
-
-
-
-
-
-
6
-
12
-
-
-
-
-
-
-
-
6
-
3
-
-
-
-
-
-
-
2
-
-
-
-
1
1
2
-
1
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
739956
Peek
The shikimate dehydrogenase fa ...
Corynebacterium glutamicum, Corynebacterium glutamicum ATCC 13032
Arch. Biochem. Biophys.
566
85-99
2015
-
2
2
2
-
-
-
5
-
-
-
6
-
4
-
-
-
4
-
-
-
-
9
2
2
2
-
-
4
2
-
-
4
-
-
-
-
2
2
4
2
-
-
-
-
-
5
-
-
-
6
-
-
-
-
-
-
-
-
9
2
2
-
-
4
2
-
-
-
-
8
8
-
-
-
740724
Guo
Molecular characterization of ...
Populus trichocarpa, Populus trichocarpa Nisqually-1
J. Biol. Chem.
289
23846-23858
2014
-
-
1
-
-
-
-
5
-
-
-
3
-
5
-
-
1
-
-
7
-
-
3
-
5
1
-
-
-
1
-
-
2
-
-
-
-
-
1
2
-
-
-
-
-
-
5
-
-
-
3
-
-
-
1
-
7
-
-
3
-
1
-
-
-
1
-
-
-
-
4
4
-
-
-
724089
Kubota
Characterization of shikimate ...
Corynebacterium glutamicum
Appl. Microbiol. Biotechnol.
97
8139-8149
2013
-
-
1
-
1
-
-
6
-
-
2
3
-
1
-
-
1
-
-
-
-
-
5
1
3
-
-
-
5
2
1
-
3
-
-
-
-
-
1
3
-
1
-
-
-
-
6
-
-
2
3
-
-
-
1
-
-
-
-
5
1
-
-
-
5
2
1
-
-
1
1
1
1
5
5
727115
Hppner
Enzyme-substrate complexes of ...
Corynebacterium glutamicum, Corynebacterium glutamicum ATCC 13032
Biol. Chem.
394
1505-1516
2013
-
-
-
1
-
-
-
8
-
-
-
5
-
7
-
-
-
-
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