BRENDA - Enzyme Database show
show all sequences of 2.7.1.49

A subfamily of bacterial ribokinases utilizes a hemithioacetal for pyridoxal phosphate salvage

Nodwell, M.B.; Koch, M.F.; Alte, F.; Schneider, S.; Sieber, S.A.; J. Am. Chem. Soc. 136, 4992-4999 (2014)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
-
Staphylococcus aureus
Crystallization (Commentary)
Crystallization
Organism
native protein and in complex with its substrates to 1.4-1.85 A resolution. The protein shows a typical ribokinase fold with a central large beta-sheet consisting of nine strands, flanked by three and five structurally conserved alpha-helices
Staphylococcus aureus
Engineering
Amino acid exchange
Commentary
Organism
C110A
residue C110 is mandatory for pyridoxal, but not for pyridoxine, or 4-amino-5-hydroxymethyl-2-methylpyrimidine turnover
Staphylococcus aureus
C214A
mutant does not turn over pyridoxal, pyridoxine, or 4-amino-5-hydroxymethyl-2-methylpyrimidine. Residue C214 acts as the catalytic base in the phosphorylation reaction
Staphylococcus aureus
Inhibitors
Inhibitors
Commentary
Organism
Structure
rugulactone
selectively modifies the enzyme not at the active site cysteine, but on a remote cysteine residue
Staphylococcus aureus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.111
-
pyridoxal
wild-type, pH not specified in the publication, temperature not specified in the publication
Staphylococcus aureus
0.26
-
pyridoxal
mutant C214D, pH not specified in the publication, temperature not specified in the publication
Staphylococcus aureus
1.51
-
pyridoxine
mutant C110A, pH not specified in the publication, temperature not specified in the publication
Staphylococcus aureus
1.85
-
4-Amino-5-hydroxymethyl-2-methylpyrimidine
mutant C110A, pH not specified in the publication, temperature not specified in the publication
Staphylococcus aureus
1.99
-
4-Amino-5-hydroxymethyl-2-methylpyrimidine
wild-type, pH not specified in the publication, temperature not specified in the publication
Staphylococcus aureus
2.07
-
pyridoxine
wild-type, pH not specified in the publication, temperature not specified in the publication
Staphylococcus aureus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Staphylococcus aureus
A0A0H3JTP0
-
-
Staphylococcus aureus ATCC 700699
A0A0H3JTP0
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine
-
738451
Staphylococcus aureus
ADP + 4-amino-5-phosphomethyl-2-methylpyrimidine
-
-
-
?
ATP + pyridoxal
reaction of EC 2.7.1.35
738451
Staphylococcus aureus
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
reaction of EC 2.7.1.35
738451
Staphylococcus aureus ATCC 700699
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxine
reaction of EC 2.7.1.35
738451
Staphylococcus aureus
ADP + pyridoxine 5'-phosphate
-
-
-
?
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.015
-
pyridoxine
mutant C110A, pH not specified in the publication, temperature not specified in the publication
Staphylococcus aureus
0.016
-
pyridoxine
wild-type, pH not specified in the publication, temperature not specified in the publication
Staphylococcus aureus
0.044
-
4-Amino-5-hydroxymethyl-2-methylpyrimidine
mutant C110A, pH not specified in the publication, temperature not specified in the publication
Staphylococcus aureus
0.045
-
4-Amino-5-hydroxymethyl-2-methylpyrimidine
wild-type, pH not specified in the publication, temperature not specified in the publication
Staphylococcus aureus
0.165
-
pyridoxal
wild-type, pH not specified in the publication, temperature not specified in the publication
Staphylococcus aureus
0.328
-
pyridoxal
mutant C214D, pH not specified in the publication, temperature not specified in the publication
Staphylococcus aureus
Cloned(Commentary) (protein specific)
Commentary
Organism
-
Staphylococcus aureus
Crystallization (Commentary) (protein specific)
Crystallization
Organism
native protein and in complex with its substrates to 1.4-1.85 A resolution. The protein shows a typical ribokinase fold with a central large beta-sheet consisting of nine strands, flanked by three and five structurally conserved alpha-helices
Staphylococcus aureus
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
C110A
residue C110 is mandatory for pyridoxal, but not for pyridoxine, or 4-amino-5-hydroxymethyl-2-methylpyrimidine turnover
Staphylococcus aureus
C214A
mutant does not turn over pyridoxal, pyridoxine, or 4-amino-5-hydroxymethyl-2-methylpyrimidine. Residue C214 acts as the catalytic base in the phosphorylation reaction
Staphylococcus aureus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
rugulactone
selectively modifies the enzyme not at the active site cysteine, but on a remote cysteine residue
Staphylococcus aureus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.111
-
pyridoxal
wild-type, pH not specified in the publication, temperature not specified in the publication
Staphylococcus aureus
0.26
-
pyridoxal
mutant C214D, pH not specified in the publication, temperature not specified in the publication
Staphylococcus aureus
1.51
-
pyridoxine
mutant C110A, pH not specified in the publication, temperature not specified in the publication
Staphylococcus aureus
1.85
-
4-Amino-5-hydroxymethyl-2-methylpyrimidine
mutant C110A, pH not specified in the publication, temperature not specified in the publication
Staphylococcus aureus
1.99
-
4-Amino-5-hydroxymethyl-2-methylpyrimidine
wild-type, pH not specified in the publication, temperature not specified in the publication
Staphylococcus aureus
2.07
-
pyridoxine
wild-type, pH not specified in the publication, temperature not specified in the publication
Staphylococcus aureus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine
-
738451
Staphylococcus aureus
ADP + 4-amino-5-phosphomethyl-2-methylpyrimidine
-
-
-
?
ATP + pyridoxal
reaction of EC 2.7.1.35
738451
Staphylococcus aureus
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
reaction of EC 2.7.1.35
738451
Staphylococcus aureus ATCC 700699
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxine
reaction of EC 2.7.1.35
738451
Staphylococcus aureus
ADP + pyridoxine 5'-phosphate
-
-
-
?
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.015
-
pyridoxine
mutant C110A, pH not specified in the publication, temperature not specified in the publication
Staphylococcus aureus
0.016
-
pyridoxine
wild-type, pH not specified in the publication, temperature not specified in the publication
Staphylococcus aureus
0.044
-
4-Amino-5-hydroxymethyl-2-methylpyrimidine
mutant C110A, pH not specified in the publication, temperature not specified in the publication
Staphylococcus aureus
0.045
-
4-Amino-5-hydroxymethyl-2-methylpyrimidine
wild-type, pH not specified in the publication, temperature not specified in the publication
Staphylococcus aureus
0.165
-
pyridoxal
wild-type, pH not specified in the publication, temperature not specified in the publication
Staphylococcus aureus
0.328
-
pyridoxal
mutant C214D, pH not specified in the publication, temperature not specified in the publication
Staphylococcus aureus
Other publictions for EC 2.7.1.49
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)
738234
Castro-Fernandez
Emergence of pyridoxal phospho ...
Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720
FEBS Lett.
588
3068-3073
2014
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2
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-
-
-
-
-
1
1
-
-
-
738451
Nodwell
A subfamily of bacterial ribok ...
Staphylococcus aureus, Staphylococcus aureus ATCC 700699
J. Am. Chem. Soc.
136
4992-4999
2014
-
-
1
1
2
-
1
6
-
-
-
-
-
2
-
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-
-
-
-
-
4
-
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6
-
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1
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1
2
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1
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6
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-
4
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6
-
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-
-
-
-
-
-
722048
Nodwell
Rugulactone and its analogues ...
Staphylococcus aureus
ChemBioChem
13
1439-1446
2012
-
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-
-
-
-
3
-
-
-
-
-
-
1
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3
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3
3
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-
718477
French
Structure of trifunctional THI ...
Saccharomyces cerevisiae
Acta Crystallogr. Sect. D
67
784-791
2011
-
-
-
1
-
-
-
-
-
-
-
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2
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-
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1
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-
686824
Onozuka
Involvement of thiaminase II e ...
Saccharomyces cerevisiae
FEMS Yeast Res.
8
266-275
2008
-
-
1
-
-
-
-
-
-
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1
-
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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1
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1
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2
-
1
-
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-
1
-
-
-
-
-
-
-
-
-
671903
Rapala-Kozik
Molecular characterization of ...
Zea mays
Biochem. J.
408
149-159
2007
-
-
1
-
7
-
-
-
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-
3
-
-
5
-
-
1
-
-
1
-
-
1
1
-
-
-
-
-
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-
1
-
1
-
-
-
1
1
-
7
-
-
-
-
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-
-
3
-
-
-
-
1
-
1
-
-
1
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
672477
Wrenger
Vitamin B1 de novo synthesis i ...
Plasmodium falciparum
Biol. Chem.
387
41-51
2006
-
-
1
-
-
-
-
2
-
-
1
-
-
1
-
-
1
-
-
-
2
-
4
1
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-
1
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-
1
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-
1
1
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-
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-
-
-
2
-
-
1
-
-
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-
1
-
-
2
-
4
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
674302
Karunakaran
Thiamine is synthesized by a s ...
Rhizobium leguminosarum
J. Bacteriol.
188
6661-6668
2006
-
-
-
-
-
-
-
-
-
-
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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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-
-
-
661316
Haas
Thi20, a remarkable enzyme fro ...
Saccharomyces cerevisiae
Bioorg. Chem.
33
338-344
2005
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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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1
-
1
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1
-
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-
-
-
-
-
-
-
661537
Kawasaki
Biosynthesis of hydroxymethylp ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae YPH500
Curr. Genet.
47
156-162
2005
-
-
1
-
1
-
-
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1
1
4
-
4
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1
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1
-
6
1
1
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1
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1
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1
1
-
1
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1
1
4
-
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1
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1
-
6
1
1
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1
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-
662007
Park
Characterization of two kinase ...
Bacillus subtilis
J. Bacteriol.
186
1571-1573
2004
-
-
1
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1
-
1
-
3
-
2
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1
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4
-
1
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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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3
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-
1
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-
4
-
1
-
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-
1
-
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-
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-
641661
Mizote
Cloning and characterization o ...
Escherichia coli, Escherichia coli BL21(DE3) (pLysS)
Microbiology
145
495-501
1999
-
-
1
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2
2
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4
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1
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1
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6
1
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2
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2
2
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1
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1
-
6
1
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-
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-
639726
Kim
A Brassica cDNA clone encoding ...
Arabidopsis thaliana, Brassica napus
Plant Mol. Biol.
37
955-966
1998
-
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2
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2
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2
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2
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3
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5
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2
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2
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2
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3
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5
-
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-
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-
641660
Reddick
-
Overexpression, purification a ...
Escherichia coli
Tetrahedron
54
15983-15991
1998
-
1
1
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3
-
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3
1
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1
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1
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1
4
1
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3
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1
1
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3
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3
1
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1
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1
4
1
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3
-
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-
641658
Mizote
Purification and properties of ...
Escherichia coli
Biochim. Biophys. Acta
991
109-113
1989
-
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2
4
1
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1
1
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2
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1
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1
1
-
5
1
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2
2
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2
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2
2
4
1
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1
1
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1
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1
1
-
5
1
-
-
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2
2
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-
641657
Lewin
-
The biosynthesis of thiamine. ...
Saccharomyces cerevisiae
J. Biol. Chem.
236
2768-2771
1961
-
-
-
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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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6
-
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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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6
-
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1
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