BRENDA - Enzyme Database show
show all sequences of 1.1.1.405

acs1 of Haemophilus influenzae type a capsulation locus region II encodes a bifunctional ribulose 5-phosphate reductase- CDP-ribitol pyrophosphorylase

Follens, A.; Veiga-da-Cunha, M.; Merckx, R.; van Schaftingen, E.; van Eldere, J.; J. Bacteriol. 181, 2001-2007 (1999)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
CTP
marked stimulation, presence of 50 mM CTP decreases the Km value for ribulose 5-phosphate from 400 to 50 microM
Haemophilus influenzae
additional information
not stimulated by UTP, ATP, GTP, ADP, or dCTP
Haemophilus influenzae
Cloned(Commentary)
Commentary
Organism
expression in ERscherichia coli
Haemophilus influenzae
General Stability
General Stability
Organism
23C, at 0.3 mg/ml in the presence of 20 mM HEPES, pH 7.1, 1 mM DTT, and 0.5 mg of BSA/ml, ribitol 5-phosphate dehydrogenase activity decreases to about 50% of the initial activity after 2 h
Haemophilus influenzae
Inhibitors
Inhibitors
Commentary
Organism
Structure
additional information
not inhibitory: 0.5 mM ribitol 5-phosphate or 0.5 mM NADP+
Haemophilus influenzae
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.01
-
NADPH
pH 7.1, 30C
Haemophilus influenzae
0.05
-
D-ribitol 5-phosphate
presence of CTP, pH 7.1, 30C
Haemophilus influenzae
0.4
-
D-ribitol 5-phosphate
pH 7.1, 30C
Haemophilus influenzae
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
53000
-
x * 53000, SDS-PAGE
Haemophilus influenzae
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Haemophilus influenzae
Q48154
additionally catalyzes reaction of ribitol-5-phosphate cytidylyltransferase, EC 2.7.7.40
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
0.73
-
substrate D-ribulose 5-phosphate, pH 8.5, 30C
Haemophilus influenzae
2.87
-
substrate D-ribulose 5-phosphate, presence of CTP, pH 8.5, 30C
Haemophilus influenzae
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-ribitol 5-phosphate + NADP+
-
645253
Haemophilus influenzae
D-ribulose 5-phosphate + NADPH + H+
-
-
-
r
D-ribulose 5-phosphate + NADPH + H+
-
645253
Haemophilus influenzae
D-ribitol 5-phosphate + NADP+
-
-
-
r
additional information
the dehydrogenase activity of Acs1 is specific for ribulose 5-phosphate and NADPH in one direction and for ribitol 5-phosphate and NADP+ in the other direction. The activity is about twofold higher with ribulose 5-phosphate as the substrate than with ribose 5-phosphate. No substrate: xylulose 5-phosphate
645253
Haemophilus influenzae
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
?
x * 53000, SDS-PAGE
Haemophilus influenzae
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
8.4
broad
Haemophilus influenzae
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
CTP
marked stimulation, presence of 50 mM CTP decreases the Km value for ribulose 5-phosphate from 400 to 50 microM
Haemophilus influenzae
additional information
not stimulated by UTP, ATP, GTP, ADP, or dCTP
Haemophilus influenzae
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in ERscherichia coli
Haemophilus influenzae
General Stability (protein specific)
General Stability
Organism
23C, at 0.3 mg/ml in the presence of 20 mM HEPES, pH 7.1, 1 mM DTT, and 0.5 mg of BSA/ml, ribitol 5-phosphate dehydrogenase activity decreases to about 50% of the initial activity after 2 h
Haemophilus influenzae
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
additional information
not inhibitory: 0.5 mM ribitol 5-phosphate or 0.5 mM NADP+
Haemophilus influenzae
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.01
-
NADPH
pH 7.1, 30C
Haemophilus influenzae
0.05
-
D-ribitol 5-phosphate
presence of CTP, pH 7.1, 30C
Haemophilus influenzae
0.4
-
D-ribitol 5-phosphate
pH 7.1, 30C
Haemophilus influenzae
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
53000
-
x * 53000, SDS-PAGE
Haemophilus influenzae
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
0.73
-
substrate D-ribulose 5-phosphate, pH 8.5, 30C
Haemophilus influenzae
2.87
-
substrate D-ribulose 5-phosphate, presence of CTP, pH 8.5, 30C
Haemophilus influenzae
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-ribitol 5-phosphate + NADP+
-
645253
Haemophilus influenzae
D-ribulose 5-phosphate + NADPH + H+
-
-
-
r
D-ribulose 5-phosphate + NADPH + H+
-
645253
Haemophilus influenzae
D-ribitol 5-phosphate + NADP+
-
-
-
r
additional information
the dehydrogenase activity of Acs1 is specific for ribulose 5-phosphate and NADPH in one direction and for ribitol 5-phosphate and NADP+ in the other direction. The activity is about twofold higher with ribulose 5-phosphate as the substrate than with ribose 5-phosphate. No substrate: xylulose 5-phosphate
645253
Haemophilus influenzae
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 53000, SDS-PAGE
Haemophilus influenzae
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
8.4
broad
Haemophilus influenzae
General Information
General Information
Commentary
Organism
physiological function
Acs1 encodes a bifunctional enzyme that converts ribulose 5-phosphate into ribitol 5-phosphate and further into CDP-ribitol, the activated precursor form for incorporation of ribitol 5-phosphate into the Haemophilus influenzae type a capsular polysaccharide
Haemophilus influenzae
General Information (protein specific)
General Information
Commentary
Organism
physiological function
Acs1 encodes a bifunctional enzyme that converts ribulose 5-phosphate into ribitol 5-phosphate and further into CDP-ribitol, the activated precursor form for incorporation of ribitol 5-phosphate into the Haemophilus influenzae type a capsular polysaccharide
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
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1
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1
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1
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1
2
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1
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1
1
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1
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650236
Pereira
Bifunctional catalysis by CDP- ...
Haemophilus influenzae, Staphylococcus aureus
Biochemistry
43
11802-11812
2004
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1
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6
4
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5
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2
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1
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2
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4
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6
2
4
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5
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2
2
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4
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645254
Zolli
Reduction precedes cytidylyl t ...
Haemophilus influenzae
Biochemistry
40
5041-5048
2001
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1
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2
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12
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1
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7
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9
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1
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12
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7
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9
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11
11
645253
Follens
acs1 of Haemophilus influenzae ...
Haemophilus influenzae
J. Bacteriol.
181
2001-2007
1999
2
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1
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1
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3
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1
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