BRENDA - Enzyme Database
show all sequences of 2.5.1.17

Spectroscopic studies of the Salmonella enterica adenosyltransferase enzyme SeCobA: molecular-level insight into the mechanism of substrate Cob(II)alamin activation

Pallares, I.G.; Moore, T.C.; Escalante-Semerena, J.C.; Brunold, T.C.; Biochemistry 53, 7969-7982 (2014)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expressed in Escherichia coli BL21 cells
Salmonella enterica
Engineering
Amino acid exchange
Commentary
Organism
F91W
with cob(II)alamin the mutant shows catalytic activity diminished relative to that of wild type enzyme, while the activity with cob(I)alamin is largely retained
Salmonella enterica
F91W/W93F
in this mutant the yield of 4c cob(II)alamin species is reduced more than 10fold from that achieved by the wild type enzyme
Salmonella enterica
F91Y
with cob(II)alamin the mutant shows catalytic activity 5fold increased relative to that of wild type enzyme
Salmonella enterica
W93A
the mutation completely abolishes the catalytic activity with cob(II)alamin while modest activity is retained with cob(I)alamin
Salmonella enterica
W93F
the mutant shows wild type activity
Salmonella enterica
W93H
the mutation inhibits the formation of 4c cob(II)alamin
Salmonella enterica
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0163
-
cob(II)inamide
wild type enzyme, pH and temperature not specified in the publication
Salmonella enterica
0.0254
-
ATP
wild type enzyme, pH and temperature not specified in the publication
Salmonella enterica
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + cob(I)yrinic acid a,c-diamide
Salmonella enterica
-
triphosphate + adenosylcob(III)yrinic acid a,c-diamide
-
-
?
ATP + cobinamide
Salmonella enterica
-
triphosphate + adenosylcobinamide
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Salmonella enterica
P31570
serovar typhimurium LT2
-
Purification (Commentary)
Commentary
Organism
HisTrap nickel affinity column chromatography
Salmonella enterica
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + cob(I)alamine
-
737702
Salmonella enterica
triphosphate + adenosylcob(I)alamine
-
-
-
?
ATP + cob(I)yrinic acid a,c-diamide
-
737702
Salmonella enterica
triphosphate + adenosylcob(III)yrinic acid a,c-diamide
-
-
-
?
ATP + cob(II)alamine
-
737702
Salmonella enterica
triphosphate + adenosylcob(II)alamine
-
-
-
?
ATP + cob(II)inamide
-
737702
Salmonella enterica
triphosphate + adenosylcob(II)inamide
-
-
-
?
ATP + cobinamide
-
737702
Salmonella enterica
triphosphate + adenosylcobinamide
-
-
-
?
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.0067
-
ATP
wild type enzyme, pH and temperature not specified in the publication
Salmonella enterica
0.0077
-
cob(II)inamide
wild type enzyme, pH and temperature not specified in the publication
Salmonella enterica
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli BL21 cells
Salmonella enterica
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
F91W
with cob(II)alamin the mutant shows catalytic activity diminished relative to that of wild type enzyme, while the activity with cob(I)alamin is largely retained
Salmonella enterica
F91W/W93F
in this mutant the yield of 4c cob(II)alamin species is reduced more than 10fold from that achieved by the wild type enzyme
Salmonella enterica
F91Y
with cob(II)alamin the mutant shows catalytic activity 5fold increased relative to that of wild type enzyme
Salmonella enterica
W93A
the mutation completely abolishes the catalytic activity with cob(II)alamin while modest activity is retained with cob(I)alamin
Salmonella enterica
W93F
the mutant shows wild type activity
Salmonella enterica
W93H
the mutation inhibits the formation of 4c cob(II)alamin
Salmonella enterica
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0163
-
cob(II)inamide
wild type enzyme, pH and temperature not specified in the publication
Salmonella enterica
0.0254
-
ATP
wild type enzyme, pH and temperature not specified in the publication
Salmonella enterica
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + cob(I)yrinic acid a,c-diamide
Salmonella enterica
-
triphosphate + adenosylcob(III)yrinic acid a,c-diamide
-
-
?
ATP + cobinamide
Salmonella enterica
-
triphosphate + adenosylcobinamide
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
HisTrap nickel affinity column chromatography
Salmonella enterica
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + cob(I)alamine
-
737702
Salmonella enterica
triphosphate + adenosylcob(I)alamine
-
-
-
?
ATP + cob(I)yrinic acid a,c-diamide
-
737702
Salmonella enterica
triphosphate + adenosylcob(III)yrinic acid a,c-diamide
-
-
-
?
ATP + cob(II)alamine
-
737702
Salmonella enterica
triphosphate + adenosylcob(II)alamine
-
-
-
?
ATP + cob(II)inamide
-
737702
Salmonella enterica
triphosphate + adenosylcob(II)inamide
-
-
-
?
ATP + cobinamide
-
737702
Salmonella enterica
triphosphate + adenosylcobinamide
-
-
-
?
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.0067
-
ATP
wild type enzyme, pH and temperature not specified in the publication
Salmonella enterica
0.0077
-
cob(II)inamide
wild type enzyme, pH and temperature not specified in the publication
Salmonella enterica
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.26
-
ATP
wild type enzyme, pH and temperature not specified in the publication
Salmonella enterica
0.47
-
cob(II)inamide
wild type enzyme, pH and temperature not specified in the publication
Salmonella enterica
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.26
-
ATP
wild type enzyme, pH and temperature not specified in the publication
Salmonella enterica
0.47
-
cob(II)inamide
wild type enzyme, pH and temperature not specified in the publication
Salmonella enterica
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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-
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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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737702
Pallares
Spectroscopic studies of the S ...
Salmonella enterica
Biochemistry
53
7969-7982
2014
-
-
1
-
6
-
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2
-
-
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2
-
3
-
-
1
-
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5
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2
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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
-
1
-
4
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1
-
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
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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
-
-
1
1
12
-
-
18
-
1
-
1
-
2
-
-
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
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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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1
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2
2
-
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704686
Mera
Dihydroflavin-driven adenosyla ...
Homo sapiens, Lactobacillus reuteri
J. Biol. Chem.
285
2911-2917
2010
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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
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8
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3
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2
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2
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1
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2
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8
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3
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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
-
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1
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7
-
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29
-
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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
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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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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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2
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1
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1
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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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690933
Fan
Functional characterization an ...
Homo sapiens
Biochemistry
47
2806-2813
2008
-
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
-
4
-
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33
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690964
St Maurice
Structural characterization of ...
Lactobacillus reuteri
Biochemistry
47
5755-5766
2008
-
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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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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702245
Park
Kinetic and spectroscopic stud ...
Lactobacillus reuteri
Biochemistry
47
9007-9015
2008
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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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1
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1
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2
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2
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2
2
674853
St.Maurice
Structural characterization of ...
Lactobacillus reuteri, Lactobacillus reuteri CRL1098
J. Biol. Chem.
282
2596-2605
2007
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-
1
1
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2
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1
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2
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5
-
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1
2
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4
-
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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1
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7
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2
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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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2
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682763
Tanaka
Molecular properties of two pr ...
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Purification and initial chara ...
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Human ATP:cob(I)alamin adenosy ...
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Leal
Identification of the human an ...
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Fonseca
The ATP:co(I)rrinoid adenosylt ...
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Fonseca
An in vitro reducing system fo ...
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Functional genomic, biochemica ...
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Purification and initial chara ...
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Debussche
Purification and partial chara ...
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Nucleotide sequence and geneti ...
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636867
Parry
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Studies of enzyme stereochemis ...
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Sato
Assay, purification and charac ...
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636866
Beck
Ribosome-associated vitamin B1 ...
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636865
Mudd
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The adenosyltransferases ...
Clostridium tetanomorphum, Propionibacterium freudenreichii subsp. shermanii
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Vitols
Enzymatic conversion of vitami ...
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