BRENDA - Enzyme Database
show all sequences of 2.5.1.17

Spectroscopic characterization of active-site variants of the PduO-type ATP:corrinoid adenosyltransferase from Lactobacillus reuteri: insights into the mechanism of four-coordinate Co(II)corrinoid formation

Park, K.; Mera, P.E.; Escalante-Semerena, J.C.; Brunold, T.C.; Inorg. Chem. 51, 4482-4494 (2012)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene pduO, recombinant overexpression of His-tagged wild-type and mutant PduOs in Escherichia coli
Lactobacillus reuteri
Engineering
Amino acid exchange
Commentary
Organism
D35N
site-directed mutagenesis
Lactobacillus reuteri
F112A
site-directed mutagenesis
Lactobacillus reuteri
F112H
site-directed mutagenesis
Lactobacillus reuteri
F187A
site-directed mutagenesis
Lactobacillus reuteri
R128K
site-directed mutagenesis
Lactobacillus reuteri
R132K
site-directed mutagenesis
Lactobacillus reuteri
S159A
site-directed mutagenesis
Lactobacillus reuteri
V186A
site-directed mutagenesis
Lactobacillus reuteri
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + cob(I)alamin
Lactobacillus reuteri
-
triphosphate + adenosylcob(I)alamine
-
-
?
ATP + cobinamide
Lactobacillus reuteri
-
triphosphate + adenosylcobinamide
-
-
?
additional information
Lactobacillus reuteri
The PduO-type ATP:corrinoid adenosyltransferase catalyzes the transfer of the adenosyl-group of ATP to Co1+-cobalamin and Co1+-cobinamide substrates to synthesize adenosylcobalamin and adenosylcobinamide, respectively
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Lactobacillus reuteri
-
gene pduO
-
Purification (Commentary)
Commentary
Organism
recombinant His-tagged wild-type and mutant PduOs from Escherichia coli by nickel affinity chromatography to over 99% homogeneity
Lactobacillus reuteri
Reaction
Reaction
Commentary
Organism
2 ATP + 2 cob(II)alamin + a reduced flavoprotein = 2 triphosphate + 2 adenosylcob(III)alamin + an oxidized flavoprotein
to overcome the thermodynamically challenging Co2+ -> Co1+ reduction, the enzyme drastically weakens the axial ligand-Co2+ bond so as to generate effectively four-coordinate Co2+-corrinoid species, mechanism, overview. The entire hydrophobic pocket below the corrin ring, and not just residue F112, is critical for the removal of the axial ligand from the cobalt center of the Co2+-corrinoids. Large role of the ATP-induced active-site conformational changes with respect to the formation of 4c Co(II)Cbl
Lactobacillus reuteri
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + cob(I)alamin
-
722386
Lactobacillus reuteri
triphosphate + adenosylcob(I)alamine
-
-
-
?
ATP + cobinamide
-
722386
Lactobacillus reuteri
triphosphate + adenosylcobinamide
-
-
-
?
additional information
The PduO-type ATP:corrinoid adenosyltransferase catalyzes the transfer of the adenosyl-group of ATP to Co1+-cobalamin and Co1+-cobinamide substrates to synthesize adenosylcobalamin and adenosylcobinamide, respectively
722386
Lactobacillus reuteri
?
-
-
-
-
additional information
to overcome the thermodynamically challenging Co2+ -> Co1+ reduction, the enzyme drastically weakens the axial ligand-Co2+ bond so as to generate effectively four-coordinate Co2+-corrinoid species, mechanism, overview. The entire hydrophobic pocket below the corrin ring, and not just residue F112, is critical for the removal of the axial ligand from the cobalt center of the Co2+-corrinoids. Large role of the ATP-induced active-site conformational changes with respect to the formation of 4c Co(II)Cbl
722386
Lactobacillus reuteri
?
-
-
-
-
Cloned(Commentary) (protein specific)
Commentary
Organism
gene pduO, recombinant overexpression of His-tagged wild-type and mutant PduOs in Escherichia coli
Lactobacillus reuteri
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
D35N
site-directed mutagenesis
Lactobacillus reuteri
F112A
site-directed mutagenesis
Lactobacillus reuteri
F112H
site-directed mutagenesis
Lactobacillus reuteri
F187A
site-directed mutagenesis
Lactobacillus reuteri
R128K
site-directed mutagenesis
Lactobacillus reuteri
R132K
site-directed mutagenesis
Lactobacillus reuteri
S159A
site-directed mutagenesis
Lactobacillus reuteri
V186A
site-directed mutagenesis
Lactobacillus reuteri
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + cob(I)alamin
Lactobacillus reuteri
-
triphosphate + adenosylcob(I)alamine
-
-
?
ATP + cobinamide
Lactobacillus reuteri
-
triphosphate + adenosylcobinamide
-
-
?
additional information
Lactobacillus reuteri
The PduO-type ATP:corrinoid adenosyltransferase catalyzes the transfer of the adenosyl-group of ATP to Co1+-cobalamin and Co1+-cobinamide substrates to synthesize adenosylcobalamin and adenosylcobinamide, respectively
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged wild-type and mutant PduOs from Escherichia coli by nickel affinity chromatography to over 99% homogeneity
Lactobacillus reuteri
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + cob(I)alamin
-
722386
Lactobacillus reuteri
triphosphate + adenosylcob(I)alamine
-
-
-
?
ATP + cobinamide
-
722386
Lactobacillus reuteri
triphosphate + adenosylcobinamide
-
-
-
?
additional information
The PduO-type ATP:corrinoid adenosyltransferase catalyzes the transfer of the adenosyl-group of ATP to Co1+-cobalamin and Co1+-cobinamide substrates to synthesize adenosylcobalamin and adenosylcobinamide, respectively
722386
Lactobacillus reuteri
?
-
-
-
-
additional information
to overcome the thermodynamically challenging Co2+ -> Co1+ reduction, the enzyme drastically weakens the axial ligand-Co2+ bond so as to generate effectively four-coordinate Co2+-corrinoid species, mechanism, overview. The entire hydrophobic pocket below the corrin ring, and not just residue F112, is critical for the removal of the axial ligand from the cobalt center of the Co2+-corrinoids. Large role of the ATP-induced active-site conformational changes with respect to the formation of 4c Co(II)Cbl
722386
Lactobacillus reuteri
?
-
-
-
-
General Information
General Information
Commentary
Organism
additional information
active-site region of wild-type and mutant PduOs complexed with Co(II)Cbl and cosubstrate ATP, structure determination and modeling, overview
Lactobacillus reuteri
General Information (protein specific)
General Information
Commentary
Organism
additional information
active-site region of wild-type and mutant PduOs complexed with Co(II)Cbl and cosubstrate ATP, structure determination and modeling, overview
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
-
-
-
-
-
-
-
-
-
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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-
-
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2
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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
-
-
2
-
-
-
2
-
3
-
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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
-
-
1
-
1
1
-
-
3
1
-
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
-
-
-
-
-
-
-
-
-
-
721682
Moore
Structural insights into the m ...
Salmonella enterica
Biochemistry
51
9647-9657
2012
-
-
1
1
12
-
-
18
-
1
-
1
-
2
-
-
1
2
-
-
-
-
1
-
1
-
-
14
1
-
-
-
-
-
-
-
-
1
-
1
12
-
-
-
-
18
-
1
-
1
-
-
-
1
-
-
-
-
1
-
1
-
-
14
1
-
-
-
-
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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-
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3
-
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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1
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4
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1
1
-
-
-
721492
Park
Crystal structure of PduO-Type ...
Bacillus cereus
Biochem. Biophys. Res. Commun.
408
417-421
2011
-
-
1
1
-
-
-
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1
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1
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1
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1
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1
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1
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1
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1
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2
1
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2
2
-
-
-
704686
Mera
Dihydroflavin-driven adenosyla ...
Homo sapiens, Lactobacillus reuteri
J. Biol. Chem.
285
2911-2917
2010
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2
-
1
-
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-
-
-
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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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2
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1
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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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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
-
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
-
-
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-
-
-
-
29
29
702311
Padovani
A rotary mechanism for coenzym ...
Methylorubrum extorquens
Biochemistry
48
5350-5357
2009
-
-
1
-
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-
-
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-
-
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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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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
-
-
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
-
32
-
-
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
-
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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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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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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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
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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 ...
Sulfurisphaera tokodaii, Sulfurisphaera tokodaii 7
Proteins
68
446-457
2007
-
-
1
1
-
3
-
-
1
-
7
-
1
6
-
-
1
1
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Fonseca
The ATP:co(I)rrinoid adenosylt ...
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Fonseca
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Purification and initial chara ...
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Purification and partial chara ...
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Parry
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Studies of enzyme stereochemis ...
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Sato
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636866
Beck
Ribosome-associated vitamin B1 ...
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636865
Mudd
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The adenosyltransferases ...
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Vitols
Enzymatic conversion of vitami ...
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