BRENDA - Enzyme Database
show all sequences of 2.5.1.17

Structural and functional analyses of the human-type corrinoid adenosyltransferase (PduO) from Lactobacillus reuteri

Mera, P.E.; St Maurice, M.; Rayment, I.; Escalante-Semerena, J.C.; Biochemistry 46, 13829-13836 (2007)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
QuickChangeXL site-directed mutagenesis performed on wild-type LrpduO in pTEV3 before expression of wild-type and variants in Escherichia coli BL21(DE3) with a rTEV protease-cleavable N-terminal hexa-His tag
Lactobacillus reuteri
Crystallization (Commentary)
Crystallization
Organism
mutants D35N (without tag) in complex with ATP and cob(II)alamin and R132K (without tag) in complex with ATP, thin plate crystals, space group P6(3), two monomers in the asymmetric unit, unit cell parameters: a, b: 65A, c: 169A, beta: 90°; vapour-diffusion under anoxic conditions, protein solution (15 mg/ml, containing ATP, hydroxycobalamin and a reducing system of NADH, FMN, and flavodoxin reductase), reservoir solution (incl. 14-16% PEG8000, pH6)
Lactobacillus reuteri
Engineering
Amino acid exchange
Commentary
Organism
D35E/R128K
reduced activity to lower extent than mutation R128K alone
Lactobacillus reuteri
D35N
230fold decrease in kcat/KM (ATP) most likely due to disruption of salt bridge with residue R128 as observed in crystal structure
Lactobacillus reuteri
D35N/R128K
similar kinetics as mutation D35N alone
Lactobacillus reuteri
D35R/R128D
reciprocal mutation to D35/R128, very high KM values did not allow for kinetic analyses at saturating substrate concentrations
Lactobacillus reuteri
R128K
kinetics similar to wild-type, R128 conserved among PduO-type ACAs, R128 and R128K build salt bridge to residue D35 of adjacent unit, mutation R128W most common in methylmalonic aciduria patients
Lactobacillus reuteri
R132K
60-80fold decrease in kcat with respect to both substrates, 300fold decrease in kcat/KM (ATP), 3000fold decrease in kcat/KM (cob(I)alamin), identical position of ATP in the crystal structure compared to wild-type, no cob(I)alamin detectable in crystal structure
Lactobacillus reuteri
S129A
mildly affected kcat and KM for both substrated
Lactobacillus reuteri
Inhibitors
Inhibitors
Commentary
Organism
Structure
cob(I)alamin
substrate inhibition at more than 0.008 mM in presence of subsaturating concentrations of ATP (0.003 mM)
Lactobacillus reuteri
cobinamide
substrate inhibition at more than 0.005 mM in presence of subsaturating concentrations of ATP (0.003 mM)
Lactobacillus reuteri
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
wild-type: KM for CTP and UTP increased relative to ATP; wild-type: KM for GTP and ITP 530-13000fold increased relative to ATP
Lactobacillus reuteri
0.0016
-
2'-deoxy-ATP
-
Lactobacillus reuteri
0.0022
-
ATP
-
Lactobacillus reuteri
1.16
-
GTP
-
Lactobacillus reuteri
22
-
CTP
-
Lactobacillus reuteri
29
-
ITP
-
Lactobacillus reuteri
40
-
UTP
-
Lactobacillus reuteri
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Lactobacillus reuteri
-
-
-
Reaction
Reaction
Commentary
Organism
2 ATP + 2 cob(II)alamin + a reduced flavoprotein = 2 triphosphate + 2 adenosylcob(III)alamin + an oxidized flavoprotein
nucleophilic attack from reduced Co1+ ion of cob(I)alamin to the C-5’ carbon of ATP, ordered substrate binding mechanism with ATP being first and essential for catalysis
Lactobacillus reuteri
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2'-deoxy-ATP + cob(I)alamin + H2O
-
690887
Lactobacillus reuteri
?
-
-
-
?
ATP + cob(I)alamin + H2O
37°C
690887
Lactobacillus reuteri
adenosylcobalamin + diphosphate + phosphate
monitoring adenosylcobalamin formation at 388 nm in continous spectrophotometric assay
-
-
?
CTP + cob(I)alamin + H2O
37°C
690887
Lactobacillus reuteri
cytidylcobalamin + diphosphate + phosphate
-
-
-
?
GTP + cob(I)alamin + H2O
37°C
690887
Lactobacillus reuteri
guanosylcobalamin + diphosphate + phosphate
-
-
-
?
ITP + cob(I)alamin + H2O
37°C
690887
Lactobacillus reuteri
inosylcobalamin + diphosphate + phosphate
-
-
-
?
additional information
TTP does not serve as substrate
690887
Lactobacillus reuteri
?
-
-
-
-
UTP + cob(I)alamin + H2O
37°C
690887
Lactobacillus reuteri
uridylcobalamin + diphosphate + phosphate
-
-
-
?
Subunits
Subunits
Commentary
Organism
trimer
wild-type and mutants D35N and R128K, revealed by gel filtration chromatography
Lactobacillus reuteri
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
additional information
-
2'-deoxy-ATP
kcat/KM: 3300 1/M*s
Lactobacillus reuteri
additional information
-
ATP
kcat/KM: 12000 1/M*s; mutant D35E/R128K, kcat/KM: 23 1/M*s; mutant D35N, kcat/KM: 52 1/M*s; mutant D35N/R128K, kcat/KM: 32 1/M*s; mutant D35R/R128D, kcat/KM: 0.014 1/M*s, at subsaturating concentrations of 30 mM ATP and 0.02 mM cob(I)alamin; mutant R128K, kcat/KM: 1800 1/M*s; mutant R132K, kcat/KM: 39 1/M*s; mutant S129A, kcat/KM: 4500 1/M*s
Lactobacillus reuteri
additional information
-
cob(I)alamin
kcat/KM: 180000 1/M*s; mutant D35E/R128K, kcat/KM: 900 1/M*s; mutant D35N, kcat/KM: 2800 1/M*s; mutant D35N/R128K, kcat/KM: 3800 1/M*s; mutant D35R/R128D, kcat/KM: 5.2 1/M*s, at subsaturating concentrations of 30 mM ATP and 0.02 mM cob(I)alamin; mutant R128K, kcat/KM: 12000 1/M*s; mutant R132K, kcat/KM: 55 1/M*s; mutant S129A, kcat/KM: 65000 1/M*s
Lactobacillus reuteri
additional information
-
CTP
kcat/KM: 0.38 1/M*s
Lactobacillus reuteri
additional information
-
GTP
kcat/KM: 18 1/M*s
Lactobacillus reuteri
additional information
-
ITP
kcat/KM: 0.65 1/M*s
Lactobacillus reuteri
additional information
-
additional information
wild-type, decreased kcat for CTP and UTP relative to ATP; wild-type, kcat for GTP and ITP is not decreased relative to ATP
Lactobacillus reuteri
additional information
-
UTP
kcat/KM: 0.048 1/M*s
Lactobacillus reuteri
0.00041
-
cob(I)alamin
mutant R132K
Lactobacillus reuteri
0.00065
-
cob(I)alamin
mutant D35R/R128D, at subsaturating concentrations of ATP 30 mM ATP and 0.02 mM cob(I)alamin
Lactobacillus reuteri
0.00195
-
UTP
-
Lactobacillus reuteri
0.0024
-
cob(I)alamin
mutant D35E/R128K
Lactobacillus reuteri
0.0038
-
ATP
mutant S129A
Lactobacillus reuteri
0.0051
-
2'-deoxy-ATP
-
Lactobacillus reuteri
0.0062
-
ATP
mutant R128K
Lactobacillus reuteri
0.0068
-
cob(I)alamin
mutant D35N
Lactobacillus reuteri
0.0084
-
ATP
mutant R132K
Lactobacillus reuteri
0.0086
-
CTP
-
Lactobacillus reuteri
0.011
-
cob(I)alamin
mutant R128K
Lactobacillus reuteri
0.014
-
cob(I)alamin
mutant D35N/R128K
Lactobacillus reuteri
0.015
-
cob(I)alamin
mutant S129A
Lactobacillus reuteri
0.019
-
ITP
-
Lactobacillus reuteri
0.021
-
GTP
-
Lactobacillus reuteri
0.024
-
cob(I)alamin
-
Lactobacillus reuteri
0.026
-
ATP
-
Lactobacillus reuteri
0.096
-
ATP
mutant D35E/R128K
Lactobacillus reuteri
0.118
-
ATP
mutant D35N
Lactobacillus reuteri
0.41
-
ATP
mutant D35N/R128K
Lactobacillus reuteri
9
-
ATP
mutant D35R/R128D, at subsaturating concentrations of 30 mM ATP and 0.02 mM cob(I)alamin
Lactobacillus reuteri
Cloned(Commentary) (protein specific)
Commentary
Organism
QuickChangeXL site-directed mutagenesis performed on wild-type LrpduO in pTEV3 before expression of wild-type and variants in Escherichia coli BL21(DE3) with a rTEV protease-cleavable N-terminal hexa-His tag
Lactobacillus reuteri
Crystallization (Commentary) (protein specific)
Crystallization
Organism
mutants D35N (without tag) in complex with ATP and cob(II)alamin and R132K (without tag) in complex with ATP, thin plate crystals, space group P6(3), two monomers in the asymmetric unit, unit cell parameters: a, b: 65A, c: 169A, beta: 90°; vapour-diffusion under anoxic conditions, protein solution (15 mg/ml, containing ATP, hydroxycobalamin and a reducing system of NADH, FMN, and flavodoxin reductase), reservoir solution (incl. 14-16% PEG8000, pH6)
Lactobacillus reuteri
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
D35E/R128K
reduced activity to lower extent than mutation R128K alone
Lactobacillus reuteri
D35N
230fold decrease in kcat/KM (ATP) most likely due to disruption of salt bridge with residue R128 as observed in crystal structure
Lactobacillus reuteri
D35N/R128K
similar kinetics as mutation D35N alone
Lactobacillus reuteri
D35R/R128D
reciprocal mutation to D35/R128, very high KM values did not allow for kinetic analyses at saturating substrate concentrations
Lactobacillus reuteri
R128K
kinetics similar to wild-type, R128 conserved among PduO-type ACAs, R128 and R128K build salt bridge to residue D35 of adjacent unit, mutation R128W most common in methylmalonic aciduria patients
Lactobacillus reuteri
R132K
60-80fold decrease in kcat with respect to both substrates, 300fold decrease in kcat/KM (ATP), 3000fold decrease in kcat/KM (cob(I)alamin), identical position of ATP in the crystal structure compared to wild-type, no cob(I)alamin detectable in crystal structure
Lactobacillus reuteri
S129A
mildly affected kcat and KM for both substrated
Lactobacillus reuteri
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
cob(I)alamin
substrate inhibition at more than 0.008 mM in presence of subsaturating concentrations of ATP (0.003 mM)
Lactobacillus reuteri
cobinamide
substrate inhibition at more than 0.005 mM in presence of subsaturating concentrations of ATP (0.003 mM)
Lactobacillus reuteri
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
wild-type: KM for CTP and UTP increased relative to ATP; wild-type: KM for GTP and ITP 530-13000fold increased relative to ATP
Lactobacillus reuteri
0.0016
-
2'-deoxy-ATP
-
Lactobacillus reuteri
0.0022
-
ATP
-
Lactobacillus reuteri
1.16
-
GTP
-
Lactobacillus reuteri
22
-
CTP
-
Lactobacillus reuteri
29
-
ITP
-
Lactobacillus reuteri
40
-
UTP
-
Lactobacillus reuteri
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2'-deoxy-ATP + cob(I)alamin + H2O
-
690887
Lactobacillus reuteri
?
-
-
-
?
ATP + cob(I)alamin + H2O
37°C
690887
Lactobacillus reuteri
adenosylcobalamin + diphosphate + phosphate
monitoring adenosylcobalamin formation at 388 nm in continous spectrophotometric assay
-
-
?
CTP + cob(I)alamin + H2O
37°C
690887
Lactobacillus reuteri
cytidylcobalamin + diphosphate + phosphate
-
-
-
?
GTP + cob(I)alamin + H2O
37°C
690887
Lactobacillus reuteri
guanosylcobalamin + diphosphate + phosphate
-
-
-
?
ITP + cob(I)alamin + H2O
37°C
690887
Lactobacillus reuteri
inosylcobalamin + diphosphate + phosphate
-
-
-
?
additional information
TTP does not serve as substrate
690887
Lactobacillus reuteri
?
-
-
-
-
UTP + cob(I)alamin + H2O
37°C
690887
Lactobacillus reuteri
uridylcobalamin + diphosphate + phosphate
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
trimer
wild-type and mutants D35N and R128K, revealed by gel filtration chromatography
Lactobacillus reuteri
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
additional information
-
2'-deoxy-ATP
kcat/KM: 3300 1/M*s
Lactobacillus reuteri
additional information
-
ATP
kcat/KM: 12000 1/M*s; mutant D35E/R128K, kcat/KM: 23 1/M*s; mutant D35N, kcat/KM: 52 1/M*s; mutant D35N/R128K, kcat/KM: 32 1/M*s; mutant D35R/R128D, kcat/KM: 0.014 1/M*s, at subsaturating concentrations of 30 mM ATP and 0.02 mM cob(I)alamin; mutant R128K, kcat/KM: 1800 1/M*s; mutant R132K, kcat/KM: 39 1/M*s; mutant S129A, kcat/KM: 4500 1/M*s
Lactobacillus reuteri
additional information
-
cob(I)alamin
kcat/KM: 180000 1/M*s; mutant D35E/R128K, kcat/KM: 900 1/M*s; mutant D35N, kcat/KM: 2800 1/M*s; mutant D35N/R128K, kcat/KM: 3800 1/M*s; mutant D35R/R128D, kcat/KM: 5.2 1/M*s, at subsaturating concentrations of 30 mM ATP and 0.02 mM cob(I)alamin; mutant R128K, kcat/KM: 12000 1/M*s; mutant R132K, kcat/KM: 55 1/M*s; mutant S129A, kcat/KM: 65000 1/M*s
Lactobacillus reuteri
additional information
-
CTP
kcat/KM: 0.38 1/M*s
Lactobacillus reuteri
additional information
-
GTP
kcat/KM: 18 1/M*s
Lactobacillus reuteri
additional information
-
ITP
kcat/KM: 0.65 1/M*s
Lactobacillus reuteri
additional information
-
additional information
wild-type, decreased kcat for CTP and UTP relative to ATP; wild-type, kcat for GTP and ITP is not decreased relative to ATP
Lactobacillus reuteri
additional information
-
UTP
kcat/KM: 0.048 1/M*s
Lactobacillus reuteri
0.00041
-
cob(I)alamin
mutant R132K
Lactobacillus reuteri
0.00065
-
cob(I)alamin
mutant D35R/R128D, at subsaturating concentrations of ATP 30 mM ATP and 0.02 mM cob(I)alamin
Lactobacillus reuteri
0.00195
-
UTP
-
Lactobacillus reuteri
0.0024
-
cob(I)alamin
mutant D35E/R128K
Lactobacillus reuteri
0.0038
-
ATP
mutant S129A
Lactobacillus reuteri
0.0051
-
2'-deoxy-ATP
-
Lactobacillus reuteri
0.0062
-
ATP
mutant R128K
Lactobacillus reuteri
0.0068
-
cob(I)alamin
mutant D35N
Lactobacillus reuteri
0.0084
-
ATP
mutant R132K
Lactobacillus reuteri
0.0086
-
CTP
-
Lactobacillus reuteri
0.011
-
cob(I)alamin
mutant R128K
Lactobacillus reuteri
0.014
-
cob(I)alamin
mutant D35N/R128K
Lactobacillus reuteri
0.015
-
cob(I)alamin
mutant S129A
Lactobacillus reuteri
0.019
-
ITP
-
Lactobacillus reuteri
0.021
-
GTP
-
Lactobacillus reuteri
0.024
-
cob(I)alamin
-
Lactobacillus reuteri
0.026
-
ATP
-
Lactobacillus reuteri
0.096
-
ATP
mutant D35E/R128K
Lactobacillus reuteri
0.118
-
ATP
mutant D35N
Lactobacillus reuteri
0.41
-
ATP
mutant D35N/R128K
Lactobacillus reuteri
9
-
ATP
mutant D35R/R128D, at subsaturating concentrations of 30 mM ATP and 0.02 mM cob(I)alamin
Lactobacillus reuteri
Other publictions for EC 2.5.1.17
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)
738459
Pallares
Spectroscopic Studies of the E ...
Salmonella enterica
J. Am. Chem. Soc.
138
3694-3704
2016
-
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2
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1
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2
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737450
Park
Unprecedented mechanism employ ...
Salmonella enterica
Angew. Chem. Int. Ed. Engl.
54
7158-7161
2015
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2
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2
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3
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737702
Pallares
Spectroscopic studies of the S ...
Salmonella enterica
Biochemistry
53
7969-7982
2014
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1
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6
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2
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2
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3
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1
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5
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1
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6
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2
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2
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1
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5
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2
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2
2
738536
Moore
The EutT enzyme of Salmonella ...
Salmonella enterica, Salmonella enterica JE6583
J. Bacteriol.
196
903-910
2014
1
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1
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4
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1
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1
1
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3
1
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1
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1
6
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
1
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1
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1
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1
6
1
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1
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721682
Moore
Structural insights into the m ...
Salmonella enterica
Biochemistry
51
9647-9657
2012
-
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1
1
12
-
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18
-
1
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1
-
2
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1
2
-
-
-
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1
-
1
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-
14
1
-
-
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1
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1
12
-
-
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18
-
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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14
1
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3
3
-
18
18
722386
Park
Spectroscopic characterization ...
Lactobacillus reuteri
Inorg. Chem.
51
4482-4494
2012
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1
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8
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3
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3
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1
1
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4
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1
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8
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3
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1
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4
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1
1
-
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-
721492
Park
Crystal structure of PduO-Type ...
Bacillus cereus
Biochem. Biophys. Res. Commun.
408
417-421
2011
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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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2
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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2
1
-
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-
-
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2
2
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-
704686
Mera
Dihydroflavin-driven adenosyla ...
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285
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2010
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2
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2
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8
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8
-
3
-
2
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2
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701946
Medina
Mutation in the cobO gene gene ...
Sinorhizobium fredii
Arch. Microbiol.
191
11-21
2009
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8
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1
1
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702286
Mera
Residue Phe112 of the human-ty ...
Lactobacillus reuteri
Biochemistry
48
3138-3145
2009
-
-
1
-
7
-
-
29
-
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-
-
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2
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-
1
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2
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1
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29
1
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1
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7
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29
-
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1
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2
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1
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29
1
-
-
-
-
-
-
-
29
29
702311
Padovani
A rotary mechanism for coenzym ...
Methylorubrum extorquens
Biochemistry
48
5350-5357
2009
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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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705758
Zhang
Ligand-binding by catalyticall ...
Homo sapiens
Mol. Genet. Metab.
98
278-284
2009
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1
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2
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1
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1
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-
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690265
Park
Crystallization and preliminar ...
Bacillus cereus
Acta Crystallogr. Sect. F
64
648-650
2008
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1
1
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3
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1
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1
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690933
Fan
Functional characterization an ...
Homo sapiens
Biochemistry
47
2806-2813
2008
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1
1
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32
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32
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2
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1
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1
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4
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33
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1
1
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32
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32
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1
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1
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4
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33
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690964
St Maurice
Structural characterization of ...
Lactobacillus reuteri
Biochemistry
47
5755-5766
2008
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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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1
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1
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1
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1
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-
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695036
Moon
Crystal structure of a PduO-ty ...
Burkholderia thailandensis
Proteins
72
1066-1070
2008
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1
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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702245
Park
Kinetic and spectroscopic stud ...
Lactobacillus reuteri
Biochemistry
47
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2008
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1
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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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2
674853
St.Maurice
Structural characterization of ...
Lactobacillus reuteri, Lactobacillus reuteri CRL1098
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282
2596-2605
2007
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2
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4
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1
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2
1
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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
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1
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4
-
1
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2
1
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675180
Erger
In vivo expression of human AT ...
Homo sapiens
J. Gene Med.
9
462-469
2007
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1
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1
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2
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682763
Tanaka
Molecular properties of two pr ...
Sulfurisphaera tokodaii, Sulfurisphaera tokodaii 7
Proteins
68
446-457
2007
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2
1
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2
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2
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1
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8
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1
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6
2
1
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1
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690887
Mera
Structural and functional anal ...
Lactobacillus reuteri
Biochemistry
46
13829-13836
2007
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1
1
7
-
2
7
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5
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1
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7
1
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29
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1
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1
7
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2
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7
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7
1
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29
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672110
Schubert
Structure of ATP-bound human A ...
Homo sapiens
Biochemistry
45
15188-15196
2006
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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
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2
1
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674277
Buan
Studies of the CobA-type ATP:C ...
Methanosarcina mazei
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3543-3550
2006
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5
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1
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1
1
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2
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1
2
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1
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2
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2
1
5
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2
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1
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1
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5
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1
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1
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674576
Buan
Purification and initial bioch ...
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281
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1
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5
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2
1
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1
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9
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1
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2
1
1
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8
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1
8
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3
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5
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3
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2
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8
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1
1
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1
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9
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1
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2
1
1
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676023
Zhang
Impact of cblB mutations on th ...
Homo sapiens
Mol. Genet. Metab.
87
315-322
2006
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2
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2
2
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3
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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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2
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5
1
1
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2
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2
2
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3
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1
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2
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658991
Stich
Spectroscopic evidence for the ...
Homo sapiens
J. Am. Chem. Soc.
127
7660-7661
2005
1
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1
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658993
Stich
Spectroscopic and computationa ...
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8710-8719
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674510
Buan
Computer-assisted docking of f ...
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J. Biol. Chem.
280
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1
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12
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1
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2
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2
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1
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2
1
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2
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12
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2
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652541
Saridakis
The structural basis for methy ...
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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
8
2
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9
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6
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2
1
1
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6
1
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659048
Buan
The eutT gene of Salmonella en ...
Salmonella enterica, Salmonella enterica subsp. enterica serovar Typhimurium
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2
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6
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2
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659058
Johnson
Purification and initial chara ...
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J. Bacteriol.
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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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3
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4
2
1
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1
1
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1
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1
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9
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3
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5
1
1
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1
1
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3
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4
2
1
-
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1
1
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659411
Leal
Human ATP:cob(I)alamin adenosy ...
Homo sapiens
J. Biol. Chem.
279
47536-47542
2004
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1
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1
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1
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636875
Leal
Identification of the human an ...
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J. Biol. Chem.
278
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2
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2
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6
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1
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3
4
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2
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2
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2
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636874
Fonseca
The ATP:co(I)rrinoid adenosylt ...
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J. Biol. Chem.
277
33127-33131
2002
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3
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1
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2
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636872
Fonseca
An in vitro reducing system fo ...
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276
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2001
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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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636873
Johnson
Functional genomic, biochemica ...
Salmonella enterica, Salmonella enterica subsp. enterica serovar Typhimurium
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1577-1584
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1
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2
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1
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3
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2
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636871
Suh
Purification and initial chara ...
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1995
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1
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1
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2
1
4
2
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1
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1
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1
1
1
-
2
-
1
-
-
-
-
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Debussche
Purification and partial chara ...
Pseudomonas denitrificans (nomen rejiciendum)
J. Bacteriol.
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6300-6302
1991
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-
-
-
-
1
3
-
1
1
3
1
-
2
-
-
1
-
-
-
4
-
6
1
1
-
-
-
1
-
-
-
-
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-
-
-
-
1
-
3
-
-
1
1
3
1
-
-
-
1
-
-
4
-
6
1
1
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-
1
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636869
Crouzet
Nucleotide sequence and geneti ...
Pseudomonas denitrificans (nomen rejiciendum)
J. Bacteriol.
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6074-6087
1991
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1
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3
-
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-
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2
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1
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2
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636867
Parry
-
Studies of enzyme stereochemis ...
Clostridium tetanomorphum
J. Am. Chem. Soc.
107
2190-2191
1985
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-
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1
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1
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1
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3
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636870
Sato
Assay, purification and charac ...
Serratia plymuthica
J. Nutr. Sci. Vitaminol.
30
405-413
1984
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-
-
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1
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2
1
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2
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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
1
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1
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2
-
1
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1
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636866
Beck
Ribosome-associated vitamin B1 ...
Clostridium tetanomorphum, Lactobacillus delbrueckii, Lactobacillus leichmannii, Propionibacterium freudenreichii subsp. shermanii
Methods Enzymol.
67
41-56
1980
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-
-
-
-
4
8
1
4
10
-
4
-
4
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1
-
-
-
1
4
10
-
2
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-
-
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4
-
8
-
1
4
10
-
4
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1
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1
4
10
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2
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636865
Mudd
-
The adenosyltransferases ...
Clostridium tetanomorphum, Propionibacterium freudenreichii subsp. shermanii
The Enzymes, 3rd. Ed. (Boyer P. D. ed. )
8
121-154
1973
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4
2
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10
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2
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2
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1
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9
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4
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2
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10
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2
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1
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9
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636864
Vitols
Enzymatic conversion of vitami ...
Clostridium tetanomorphum
J. Biol. Chem.
241
1455-1461
1966
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2
5
2
1
5
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1
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1
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1
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3
4
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1
-
1
-
1
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2
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5
-
2
1
5
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1
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1
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3
4
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1
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1
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1
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