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show all sequences of 1.1.1.405

Bifunctional catalysis by CDP-ribitol synthase: convergent recruitment of the reductase and cytidylyltransferase activities in Haemophilus influenzae and Staphylococcus aureus

Pereira, M.P.; Brown, E.D.; Biochemistry 43, 11802-11812 (2004)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
overexpression of TarI and TarJ individually from their respective genes using the T7 expression system
Staphylococcus aureus
Inhibitors
Inhibitors
Commentary
Organism
Structure
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxo-2-thiazol-2-yl-ethyl)-acetamide
-
Haemophilus influenzae
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxo-2-thiazol-2-yl-ethyl)-acetamide
-
Staphylococcus aureus
D-ribitol 5-phosphate
-
Haemophilus influenzae
D-ribitol 5-phosphate
-
Staphylococcus aureus
NADP+
competitive versus NADPH
Haemophilus influenzae
NADP+
competitive versus NADPH
Staphylococcus aureus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.00674
-
NADPH
-
Staphylococcus aureus
0.00706
-
NADPH
-
Haemophilus influenzae
0.0285
-
ribulose 5-phosphate
-
Staphylococcus aureus
0.106
-
ribulose 5-phosphate
-
Haemophilus influenzae
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
26000
-
2 * 26000 + 2 * 41000, tarI encodes an orthologue of the cytidylyltransferase domain of Bcs1 from Haemophilus influenzae and tarJ encodes an analogue of the reductase domain of Bcs1, TarI and TyrJ form a functional CDP-ribitol synthase complex, SDS-PAGE
Staphylococcus aureus
41000
-
2 * 26000 + 2 * 41000, tarI encodes an orthologue of the cytidylyltransferase domain of Bcs1 from Haemophilus influenzae and tarJ encodes an analogue of the reductase domain of Bcs1, TarI and TyrJ form a functional CDP-ribitol synthase complex, SDS-PAGE
Staphylococcus aureus
53190
-
2 * 53190, calculation from amino acid composition
Haemophilus influenzae
106400
-
amino acid composition
Haemophilus influenzae
129000
-
calculation from gel filtration and sedimentation velocity data
Staphylococcus aureus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Haemophilus influenzae
-
-
-
Staphylococcus aureus
-
-
-
Purification (Commentary)
Commentary
Organism
-
Staphylococcus aureus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-ribulose 5-phosphate + NADPH + H+
tarI encodes an orthologue of the cytidylyltransferase domain of Bcs1 from Haemophilus influenzae and tarJ encodes an analogue of the reductase domain of Bcs1, TarI and TyrJ form a functional CDP-ribitol synthase complex. Release and free diffusion of the intermediate ribitol 5-phosphate without channelling between active sites, ordered bi-bi mechanism
650236
Staphylococcus aureus
D-ribitol 5-phosphate + NADP+
-
650236
Staphylococcus aureus
?
D-ribulose 5-phosphate + NADPH + H+
the data suggest that NADPH binds first and ribulose 5-phosphate binds second. Bifunction enzyme catalyzing the reactions of EC 1.1.1.137 and EC 2.7.7.40, ordered bi-bi mechanism
650236
Haemophilus influenzae
D-ribitol 5-phosphate + NADP+
-
650236
Haemophilus influenzae
?
Subunits
Subunits
Commentary
Organism
?
2 * 26000 + 2 * 41000, tarI encodes an orthologue of the cytidylyltransferase domain of Bcs1 from Haemophilus influenzae and tarJ encodes an analogue of the reductase domain of Bcs1, TarI and TyrJ form a functional CDP-ribitol synthase complex, SDS-PAGE
Staphylococcus aureus
dimer
2 * 53190, calculation from amino acid composition
Haemophilus influenzae
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.03
0.55
NADPH
-
Haemophilus influenzae
0.79
-
NADPH
-
Staphylococcus aureus
6.08
-
NADPH
-
Staphylococcus aureus
7.41
-
NADPH
-
Haemophilus influenzae
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
additional information
-
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxo-2-thiazol-2-yl-ethyl)-acetamide
Ki(intercept) and Ki(slope)-values
Haemophilus influenzae
additional information
-
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxo-2-thiazol-2-yl-ethyl)-acetamide
Ki(intercept) and Ki(slope)-values
Staphylococcus aureus
Cloned(Commentary) (protein specific)
Commentary
Organism
overexpression of TarI and TarJ individually from their respective genes using the T7 expression system
Staphylococcus aureus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxo-2-thiazol-2-yl-ethyl)-acetamide
-
Haemophilus influenzae
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxo-2-thiazol-2-yl-ethyl)-acetamide
-
Staphylococcus aureus
D-ribitol 5-phosphate
-
Haemophilus influenzae
D-ribitol 5-phosphate
-
Staphylococcus aureus
NADP+
competitive versus NADPH
Haemophilus influenzae
NADP+
competitive versus NADPH
Staphylococcus aureus
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
additional information
-
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxo-2-thiazol-2-yl-ethyl)-acetamide
Ki(intercept) and Ki(slope)-values
Haemophilus influenzae
additional information
-
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxo-2-thiazol-2-yl-ethyl)-acetamide
Ki(intercept) and Ki(slope)-values
Staphylococcus aureus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.00674
-
NADPH
-
Staphylococcus aureus
0.00706
-
NADPH
-
Haemophilus influenzae
0.0285
-
ribulose 5-phosphate
-
Staphylococcus aureus
0.106
-
ribulose 5-phosphate
-
Haemophilus influenzae
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
26000
-
2 * 26000 + 2 * 41000, tarI encodes an orthologue of the cytidylyltransferase domain of Bcs1 from Haemophilus influenzae and tarJ encodes an analogue of the reductase domain of Bcs1, TarI and TyrJ form a functional CDP-ribitol synthase complex, SDS-PAGE
Staphylococcus aureus
41000
-
2 * 26000 + 2 * 41000, tarI encodes an orthologue of the cytidylyltransferase domain of Bcs1 from Haemophilus influenzae and tarJ encodes an analogue of the reductase domain of Bcs1, TarI and TyrJ form a functional CDP-ribitol synthase complex, SDS-PAGE
Staphylococcus aureus
53190
-
2 * 53190, calculation from amino acid composition
Haemophilus influenzae
106400
-
amino acid composition
Haemophilus influenzae
129000
-
calculation from gel filtration and sedimentation velocity data
Staphylococcus aureus
Purification (Commentary) (protein specific)
Commentary
Organism
-
Staphylococcus aureus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-ribulose 5-phosphate + NADPH + H+
tarI encodes an orthologue of the cytidylyltransferase domain of Bcs1 from Haemophilus influenzae and tarJ encodes an analogue of the reductase domain of Bcs1, TarI and TyrJ form a functional CDP-ribitol synthase complex. Release and free diffusion of the intermediate ribitol 5-phosphate without channelling between active sites, ordered bi-bi mechanism
650236
Staphylococcus aureus
D-ribitol 5-phosphate + NADP+
-
650236
Staphylococcus aureus
?
D-ribulose 5-phosphate + NADPH + H+
the data suggest that NADPH binds first and ribulose 5-phosphate binds second. Bifunction enzyme catalyzing the reactions of EC 1.1.1.137 and EC 2.7.7.40, ordered bi-bi mechanism
650236
Haemophilus influenzae
D-ribitol 5-phosphate + NADP+
-
650236
Haemophilus influenzae
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
2 * 26000 + 2 * 41000, tarI encodes an orthologue of the cytidylyltransferase domain of Bcs1 from Haemophilus influenzae and tarJ encodes an analogue of the reductase domain of Bcs1, TarI and TyrJ form a functional CDP-ribitol synthase complex, SDS-PAGE
Staphylococcus aureus
dimer
2 * 53190, calculation from amino acid composition
Haemophilus influenzae
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.03
0.55
NADPH
-
Haemophilus influenzae
0.79
-
NADPH
-
Staphylococcus aureus
6.08
-
NADPH
-
Staphylococcus aureus
7.41
-
NADPH
-
Haemophilus influenzae
Other publictions for EC 1.1.1.405
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)
698603
Baur
Synthesis of CDP-activated rib ...
Streptococcus pneumoniae
J. Bacteriol.
191
1200-1210
2009
-
-
1
-
-
-
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
1
1
-
-
-
-
1
-
-
-
2
-
-
-
-
-
1
2
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
-
-
1
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
650236
Pereira
Bifunctional catalysis by CDP- ...
Haemophilus influenzae, Staphylococcus aureus
Biochemistry
43
11802-11812
2004
-
-
1
-
-
-
6
4
-
-
5
-
-
2
-
-
1
-
-
-
-
-
2
2
-
-
-
4
-
-
-
-
2
-
-
-
-
1
-
-
-
-
-
6
2
4
-
-
5
-
-
-
-
1
-
-
-
-
2
2
-
-
-
4
-
-
-
-
-
-
-
-
-
-
645254
Zolli
Reduction precedes cytidylyl t ...
Haemophilus influenzae
Biochemistry
40
5041-5048
2001
-
-
1
-
2
-
-
12
-
-
-
-
-
1
-
-
-
-
-
-
-
-
7
-
-
-
-
9
-
-
-
-
-
-
-
-
-
1
-
-
2
-
-
-
-
12
-
-
-
-
-
-
-
-
-
-
-
-
7
-
-
-
-
9
-
-
-
-
-
-
-
-
11
11
645253
Follens
acs1 of Haemophilus influenzae ...
Haemophilus influenzae
J. Bacteriol.
181
2001-2007
1999
2
-
1
-
-
1
1
3
-
-
1
-
-
1
-
-
-
-
-
-
2
-
3
1
-
-
-
-
1
-
-
-
-
-
-
2
-
1
-
-
-
1
-
1
-
3
-
-
1
-
-
-
-
-
-
-
2
-
3
1
-
-
-
-
1
-
-
-
-
1
1
-
-
-