BRENDA - Enzyme Database show
show all sequences of 4.1.1.11

An activator for pyruvoyl-dependent l-aspartate alpha-decarboxylase is conserved in a small group of the gamma-proteobacteria including Escherichia coli

Nozaki, S.; Webb, M.E.; Niki, H.; MicrobiologyOpen 1, 298-310 (2012)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
PanZ
PanD is activated by the putative acetyltransferase YhhK, termed PanZ. Activation of PanD both in vivo and in vitro is PanZ-dependent. PanZ binds to PanD. Gene panZ is conserved only in Escherichia coli-related enterobacterial species including Shigella, Salmonella, Klebsiella and Yersinia
Escherichia coli
Cloned(Commentary)
Commentary
Organism
gene panD, phylogenetic tree, expression of nontagged enzyme in Escherichia coli panZ-deficient strain SN227, expression of His-tagged wild-type and mutant enzymes in Escherichia coli, expression of flag3-tagged enzyme from gene panD with the cat gene inserted between frt sites in Escherichia coli strain MG1655
Escherichia coli
Engineering
Amino acid exchange
Commentary
Organism
additional information
generation of diverse panD deletion mutant strains, overview
Escherichia coli
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-aspartate
Escherichia coli
-
beta-alanine + CO2
-
-
?
L-aspartate
Escherichia coli MG1655
-
beta-alanine + CO2
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
-
gene panD
-
Escherichia coli MG1655
-
gene panD
-
Posttranslational Modification
Posttranslational Modification
Commentary
Organism
proteolytic modification
PanD is activated by the putative acetyltransferase YhhK, termed PanZ. Activation of PanD both in vivo and in vitro is PanZ-dependent. PanZ binds to PanD, cleavage of the recombinant FLAG-tag PanD by recombinant His-tagged PanZ
Escherichia coli
Purification (Commentary)
Commentary
Organism
recombinant nontagged enzyme in Escherichia coli panZ-deficient strain SN227 by ultrafiltration, ammonium sulfate fractionation, dialysis, and anionexchange chromatography, recombinant His-tagged wild-type and mutant enzymes and flag3-tagged enzyme from Escherichia coli strain MG1655 by affinity chromatography and dialysis
Escherichia coli
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-aspartate
-
728266
Escherichia coli
beta-alanine + CO2
-
-
-
?
L-aspartate
-
728266
Escherichia coli MG1655
beta-alanine + CO2
-
-
-
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Escherichia coli
Cofactor
Cofactor
Commentary
Organism
Structure
pyruvoyl cofactor
dependent on, the enzyme contains a covalently-bound pyruvoyl cofactor
Escherichia coli
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
PanZ
PanD is activated by the putative acetyltransferase YhhK, termed PanZ. Activation of PanD both in vivo and in vitro is PanZ-dependent. PanZ binds to PanD. Gene panZ is conserved only in Escherichia coli-related enterobacterial species including Shigella, Salmonella, Klebsiella and Yersinia
Escherichia coli
Cloned(Commentary) (protein specific)
Commentary
Organism
gene panD, phylogenetic tree, expression of nontagged enzyme in Escherichia coli panZ-deficient strain SN227, expression of His-tagged wild-type and mutant enzymes in Escherichia coli, expression of flag3-tagged enzyme from gene panD with the cat gene inserted between frt sites in Escherichia coli strain MG1655
Escherichia coli
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
pyruvoyl cofactor
dependent on, the enzyme contains a covalently-bound pyruvoyl cofactor
Escherichia coli
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
generation of diverse panD deletion mutant strains, overview
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-aspartate
Escherichia coli
-
beta-alanine + CO2
-
-
?
L-aspartate
Escherichia coli MG1655
-
beta-alanine + CO2
-
-
?
Posttranslational Modification (protein specific)
Posttranslational Modification
Commentary
Organism
proteolytic modification
PanD is activated by the putative acetyltransferase YhhK, termed PanZ. Activation of PanD both in vivo and in vitro is PanZ-dependent. PanZ binds to PanD, cleavage of the recombinant FLAG-tag PanD by recombinant His-tagged PanZ
Escherichia coli
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant nontagged enzyme in Escherichia coli panZ-deficient strain SN227 by ultrafiltration, ammonium sulfate fractionation, dialysis, and anionexchange chromatography, recombinant His-tagged wild-type and mutant enzymes and flag3-tagged enzyme from Escherichia coli strain MG1655 by affinity chromatography and dialysis
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-aspartate
-
728266
Escherichia coli
beta-alanine + CO2
-
-
-
?
L-aspartate
-
728266
Escherichia coli MG1655
beta-alanine + CO2
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Escherichia coli
General Information
General Information
Commentary
Organism
evolution
the enzyme is a member of the small class of pyruvoyl-dependent enzymes, which contain a covalently-bound pyruvoyl cofactor
Escherichia coli
metabolism
the enzyme catalyzes the first step in the biosynthetic pathway of pantothenate and coenzyme A, overview
Escherichia coli
physiological function
regulation of PanD by PanZ allows these organisms to closely regulate production of beta-alanine and hence pantothenate in response to metabolic demand in host gut flora, where pantothenate is abundant
Escherichia coli
General Information (protein specific)
General Information
Commentary
Organism
evolution
the enzyme is a member of the small class of pyruvoyl-dependent enzymes, which contain a covalently-bound pyruvoyl cofactor
Escherichia coli
metabolism
the enzyme catalyzes the first step in the biosynthetic pathway of pantothenate and coenzyme A, overview
Escherichia coli
physiological function
regulation of PanD by PanZ allows these organisms to closely regulate production of beta-alanine and hence pantothenate in response to metabolic demand in host gut flora, where pantothenate is abundant
Escherichia coli
Other publictions for EC 4.1.1.11
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)
749207
Zhang
-
Glu56Ser mutation improves th ...
Bacillus subtilis, Bacillus subtilis 168, Corynebacterium glutamicum, Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025, Escherichia coli, Lactobacillus plantarum, Lactobacillus plantarum ATCC BAA-793 / NCIMB 8826 / WCFS1
Process Biochem.
70
117-123
2018
-
-
3
-
3
-
-
-
-
-
-
7
-
11
-
4
3
-
-
-
6
-
7
4
3
3
-
-
3
3
-
-
-
4
-
-
-
3
-
-
3
-
-
-
-
-
-
-
-
7
-
-
4
3
-
-
6
-
7
4
3
3
-
-
3
3
-
4
-
10
10
-
-
-
746598
Gopal
In vivo-selected pyrazinoic a ...
Mycobacterium tuberculosis
ACS Infect. Dis.
3
492-501
2017
-
-
-
-
18
-
-
-
-
-
-
-
-
5
-
-
-
-
-
-
-
-
-
-
-
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-
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-
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-
-
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18
-
-
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-
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-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
746859
Pei
Molecular engineering of L-as ...
Bacillus subtilis 168, Bacillus subtilis, Corynebacterium glutamicum, Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025, Escherichia coli, Escherichia coli K-12 / DH5alpha
Appl. Microbiol. Biotechnol.
101
6015-6021
2017
-
-
3
-
2
-
2
6
-
-
-
6
-
10
-
3
3
-
-
-
-
-
12
-
3
2
6
3
3
-
-
1
-
-
-
-
-
3
1
-
2
-
-
2
-
6
-
-
-
6
-
-
3
3
-
-
-
-
12
-
3
2
6
3
3
-
-
-
-
-
-
-
3
3
747128
Arnott
The mechanism of regulation o ...
Escherichia coli
Biochemistry
56
4931-4939
2017
1
1
1
1
4
-
2
-
-
-
-
1
-
2
-
1
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
1
1
1
1
1
4
-
-
2
-
-
-
-
-
1
-
-
1
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
4
4
-
-
-
747799
Gliessman
Pantothenate auxotrophy in Zy ...
Escherichia coli, no activity in Zymomonas mobilis, no activity in Zymomonas mobilis ZM4 / ATCC 31821 / CP4
FEMS Microbiol. Lett.
364
fnx113
2017
-
-
1
-
-
-
-
-
-
-
-
1
-
7
-
-
-
-
-
-
-
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1
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1
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1
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1
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-
747435
Stuecker
Phylogenetic and amino acid c ...
Bacillus halodurans, Bacillus halodurans ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125, Bordetella pertussis, Bordetella pertussis Tohama I / ATCC BAA-589 / NCTC 13251, Corynebacterium glutamicum, Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025, Helicobacter pylori, Helicobacter pylori 26695, Klebsiella pneumoniae, Klebsiella pneumoniae ATCC 700721 / MGH 78578, Legionella pneumophila, Magnetospirillum magneticum, Magnetospirillum magneticum AMB-1 / ATCC 700264, Moorella thermoacetica, Moorella thermoacetica ATCC 39073 / JCM 9320, Neisseria gonorrhoeae, Neisseria gonorrhoeae ATCC 700825 / FA 1090, Pseudomonas aeruginosa, Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1, Ralstonia solanacearum, Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium LT2 / SGSC1412 / ATCC 700720
BMC Res. Notes
8
354
2015
-
-
12
-
1
-
-
-
-
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22
-
24
-
12
-
-
-
1
-
-
22
-
-
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-
-
-
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3
-
-
-
-
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12
3
-
1
-
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22
-
-
12
-
-
1
-
-
22
-
-
-
-
-
-
-
-
-
-
15
15
-
-
-
747497
Monteiro
The structure of the PanD/Pan ...
Escherichia coli
Chem. Biol.
22
492-503
2015
2
-
-
1
1
-
2
-
-
-
-
-
-
1
-
1
-
-
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1
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2
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1
1
1
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1
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-
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-
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4
4
-
-
-
747593
Deng
Characterization of L-asparta ...
Bacillus subtilis 168, Bacillus subtilis, Corynebacterium glutamicum, Corynebacterium glutamicum DSM 20300, Escherichia coli
Chin. J. Biotechnol.
31
1184-1193
2015
1
3
-
-
-
-
-
-
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5
-
7
-
3
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-
-
-
3
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5
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2
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2
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1
3
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5
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3
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3
-
5
-
2
-
-
-
2
-
-
-
-
-
-
-
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749304
Dai
Aspartate decarboxylase is re ...
Bombyx mori
Sci. Rep.
5
10885
2015
-
-
1
-
1
-
-
-
-
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1
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5
-
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4
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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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1
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4
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1
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-
-
-
-
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3
3
-
-
-
726592
Webb
-
Threonine 57 is required for t ...
Escherichia coli
Acta Crystallogr. Sect. D
70
1166-1172
2014
1
-
-
1
7
-
-
-
-
-
-
1
-
1
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1
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-
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1
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1
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1
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1
1
7
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1
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1
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1
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-
-
-
-
-
-
-
-
3
3
-
-
-
727234
Cui
Significance of Arg3, Arg54, a ...
Corynebacterium glutamicum, Corynebacterium glutamicum ATCC 13032
Biotechnol. Lett.
36
121-126
2014
-
-
1
-
10
-
-
-
-
-
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2
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4
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1
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5
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4
1
1
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1
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1
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10
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2
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1
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-
5
-
4
1
1
-
-
-
1
-
-
-
-
1
1
-
-
-
727235
Shen
Synthesis of beta-alanine from ...
Corynebacterium glutamicum, Corynebacterium glutamicum ATCC 13032
Biotechnol. Lett.
36
1681-1686
2014
-
-
1
-
-
-
1
-
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2
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4
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1
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3
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4
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1
1
1
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1
1
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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3
-
4
-
1
1
1
-
1
1
1
-
-
-
-
-
-
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727784
Wang
beta-Alanine biosynthesis in M ...
Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661
J. Bacteriol.
196
2869-2875
2014
-
-
1
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1
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2
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6
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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
1
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747380
Shen
Synthesis of beta-alanine fro ...
Corynebacterium glutamicum, Corynebacterium glutamicum ATCC 13032
Biotechnol. Lett.
36
1681-1686
2014
-
-
1
-
1
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2
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4
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1
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1
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1
1
3
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1
1
2
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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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2
-
1
1
3
-
1
1
2
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748086
Tomita
An archaeal glutamate decarbo ...
Thermococcus kodakarensis, Thermococcus kodakarensis ATCC BAA-918 / JCM 12380 / KOD1
J. Bacteriol.
196
1222-1230
2014
-
-
1
-
1
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1
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4
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7
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1
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6
2
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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6
2
1
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1
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3
3
-
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744560
Lee
-
Gene expression and character ...
Pyrococcus furiosus
Biotechnol. Bioprocess Eng.
18
375-381
2013
-
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1
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1
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4
2
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1
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2
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1
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1
1
1
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1
1
726617
Webb
Structure of Escherichia coli ...
Escherichia coli
Acta Crystallogr. Sect. F
68
414-417
2012
-
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1
1
1
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1
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1
1
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726873
Monteiro
Formation of a heterooctameric ...
Escherichia coli
Biochem. Biophys. Res. Commun.
426
350-355
2012
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
1
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727622
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