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show all sequences of 1.1.1.405

Reduction precedes cytidylyl transfer without substrate channeling in distinct active sites of the bifunctional CDP-ribitol synthase from Haemophilus influenzae

Zolli, M.; Kobric, D.J.; Brown, E.D.; Biochemistry 40, 5041-5048 (2001)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Haemophilus influenzae
Engineering
Amino acid exchange
Commentary
Organism
K386A
mutant impaired for reduction of D-ribulose. Equimolar mixtures of mutants K386A and R18A are efficient for bifunctional catalysis
Haemophilus influenzae
R18A
mutant impaired for cytidylyl transfer. Equimolar mixtures of mutants K386A and R18A are efficient for bifunctional catalysis
Haemophilus influenzae
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.017
-
NADPH
mutant R18A, pH 7.2, 25C
Haemophilus influenzae
0.038
-
(2R,3R)-2,3-dihydroxy-4-oxobutyl-phosphate
wild-type, pH 7.2, 25C
Haemophilus influenzae
0.039
-
NADPH
mutant K386A, pH 7.2, 25C
Haemophilus influenzae
0.044
-
NADPH
wild-type, pH 7.2, 25C
Haemophilus influenzae
0.076
-
D-ribulose 5-phosphate
wild-type, pH 7.2, 25C
Haemophilus influenzae
0.19
-
D-ribulose 5-phosphate
mutant K386A, pH 7.2, 25C
Haemophilus influenzae
0.27
-
D-ribulose 5-phosphate
mutant R18A, pH 7.2, 25C
Haemophilus influenzae
0.6
-
NADH
wild-type, pH 7.2, 25C
Haemophilus influenzae
1.1
-
D-ribulose
wild-type, pH 7.2, 25C
Haemophilus influenzae
2.2
-
D-ribose 5-phosphate
wild-type, pH 7.2, 25C
Haemophilus influenzae
3
-
D-arabinose 5-phosphate
wild-type, pH 7.2, 25C
Haemophilus influenzae
3.5
-
D-xylulose 5-phosphate
wild-type, pH 7.2, 25C
Haemophilus influenzae
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Haemophilus influenzae
Q48230
additionally catalyzes the reaction of ribitol-5-phosphate cytidylyltransferase, EC 2.7.7.40
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-arabinose 5-phosphate + NADPH + H+
-
645254
Haemophilus influenzae
? + NADP+
-
-
-
?
D-erythrose 4-phosphate + NADPH + H+
-
645254
Haemophilus influenzae
? + NADP+
-
-
-
?
D-ribose 5-phosphate + NADPH + H+
-
645254
Haemophilus influenzae
? + NADP+
-
-
-
?
D-ribulose + NADPH + H+
-
645254
Haemophilus influenzae
D-ribitol + NADP+
-
-
-
?
D-ribulose 5-phosphate + NADPH + H+
-
645254
Haemophilus influenzae
D-ribitol 5-phosphate + NADP+
-
-
-
?
D-xylulose 5-phosphate + NADH + H+
-
645254
Haemophilus influenzae
? + NAD+
-
-
-
?
additional information
the synthase first catalyzes the reduction of D-ribulose 5-phosphate followed by cytidylyl transfer to D-ribitol 5-phosphate, with a 650fold kinetic preference for cytidylyl transfer to D-ribitol 5-phosphate over D-ribulose 5-phosphate
645254
Haemophilus influenzae
?
-
-
-
-
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.32
-
D-ribulose 5-phosphate
mutant K386A, pH 7.2, 25C
Haemophilus influenzae
0.5
-
(2R,3R)-2,3-dihydroxy-4-oxobutyl-phosphate
wild-type, pH 7.2, 25C
Haemophilus influenzae
2.3
-
D-arabinose 5-phosphate
wild-type, pH 7.2, 25C
Haemophilus influenzae
3.6
-
D-ribulose
wild-type, pH 7.2, 25C
Haemophilus influenzae
3.6
-
D-xylulose 5-phosphate
wild-type, pH 7.2, 25C
Haemophilus influenzae
4.1
-
D-ribose 5-phosphate
wild-type, pH 7.2, 25C
Haemophilus influenzae
6.8
-
D-ribulose 5-phosphate
mutant R18A, pH 7.2, 25C
Haemophilus influenzae
22
-
D-ribulose 5-phosphate
wild-type, pH 7.2, 25C
Haemophilus influenzae
22
-
NADPH
wild-type, pH 7.2, 25C
Haemophilus influenzae
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Haemophilus influenzae
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
K386A
mutant impaired for reduction of D-ribulose. Equimolar mixtures of mutants K386A and R18A are efficient for bifunctional catalysis
Haemophilus influenzae
R18A
mutant impaired for cytidylyl transfer. Equimolar mixtures of mutants K386A and R18A are efficient for bifunctional catalysis
Haemophilus influenzae
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.017
-
NADPH
mutant R18A, pH 7.2, 25C
Haemophilus influenzae
0.038
-
(2R,3R)-2,3-dihydroxy-4-oxobutyl-phosphate
wild-type, pH 7.2, 25C
Haemophilus influenzae
0.039
-
NADPH
mutant K386A, pH 7.2, 25C
Haemophilus influenzae
0.044
-
NADPH
wild-type, pH 7.2, 25C
Haemophilus influenzae
0.076
-
D-ribulose 5-phosphate
wild-type, pH 7.2, 25C
Haemophilus influenzae
0.19
-
D-ribulose 5-phosphate
mutant K386A, pH 7.2, 25C
Haemophilus influenzae
0.27
-
D-ribulose 5-phosphate
mutant R18A, pH 7.2, 25C
Haemophilus influenzae
0.6
-
NADH
wild-type, pH 7.2, 25C
Haemophilus influenzae
1.1
-
D-ribulose
wild-type, pH 7.2, 25C
Haemophilus influenzae
2.2
-
D-ribose 5-phosphate
wild-type, pH 7.2, 25C
Haemophilus influenzae
3
-
D-arabinose 5-phosphate
wild-type, pH 7.2, 25C
Haemophilus influenzae
3.5
-
D-xylulose 5-phosphate
wild-type, pH 7.2, 25C
Haemophilus influenzae
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-arabinose 5-phosphate + NADPH + H+
-
645254
Haemophilus influenzae
? + NADP+
-
-
-
?
D-erythrose 4-phosphate + NADPH + H+
-
645254
Haemophilus influenzae
? + NADP+
-
-
-
?
D-ribose 5-phosphate + NADPH + H+
-
645254
Haemophilus influenzae
? + NADP+
-
-
-
?
D-ribulose + NADPH + H+
-
645254
Haemophilus influenzae
D-ribitol + NADP+
-
-
-
?
D-ribulose 5-phosphate + NADPH + H+
-
645254
Haemophilus influenzae
D-ribitol 5-phosphate + NADP+
-
-
-
?
D-xylulose 5-phosphate + NADH + H+
-
645254
Haemophilus influenzae
? + NAD+
-
-
-
?
additional information
the synthase first catalyzes the reduction of D-ribulose 5-phosphate followed by cytidylyl transfer to D-ribitol 5-phosphate, with a 650fold kinetic preference for cytidylyl transfer to D-ribitol 5-phosphate over D-ribulose 5-phosphate
645254
Haemophilus influenzae
?
-
-
-
-
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.32
-
D-ribulose 5-phosphate
mutant K386A, pH 7.2, 25C
Haemophilus influenzae
0.5
-
(2R,3R)-2,3-dihydroxy-4-oxobutyl-phosphate
wild-type, pH 7.2, 25C
Haemophilus influenzae
2.3
-
D-arabinose 5-phosphate
wild-type, pH 7.2, 25C
Haemophilus influenzae
3.6
-
D-ribulose
wild-type, pH 7.2, 25C
Haemophilus influenzae
3.6
-
D-xylulose 5-phosphate
wild-type, pH 7.2, 25C
Haemophilus influenzae
4.1
-
D-ribose 5-phosphate
wild-type, pH 7.2, 25C
Haemophilus influenzae
6.8
-
D-ribulose 5-phosphate
mutant R18A, pH 7.2, 25C
Haemophilus influenzae
22
-
D-ribulose 5-phosphate
wild-type, pH 7.2, 25C
Haemophilus influenzae
22
-
NADPH
wild-type, pH 7.2, 25C
Haemophilus influenzae
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.00008
-
D-arabinose 5-phosphate
wild-type, pH 7.2, 25C
Haemophilus influenzae
0.0001
-
D-xylulose 5-phosphate
wild-type, pH 7.2, 25C
Haemophilus influenzae
0.0002
-
D-ribose 5-phosphate
wild-type, pH 7.2, 25C
Haemophilus influenzae
0.0002
-
D-ribulose 5-phosphate
mutant K386A, pH 7.2, 25C
Haemophilus influenzae
0.0003
-
D-ribulose
wild-type, pH 7.2, 25C
Haemophilus influenzae
0.0008
-
NADPH
mutant K386A, pH 7.2, 25C
Haemophilus influenzae
0.0013
-
(2R,3R)-2,3-dihydroxy-4-oxobutyl-phosphate
wild-type, pH 7.2, 25C
Haemophilus influenzae
0.0025
-
D-ribulose 5-phosphate
mutant R18A, pH 7.2, 25C
Haemophilus influenzae
0.029
-
D-ribulose 5-phosphate
wild-type, pH 7.2, 25C
Haemophilus influenzae
0.04
-
NADPH
mutant R18A, pH 7.2, 25C
Haemophilus influenzae
0.05
-
NADPH
wild-type, pH 7.2, 25C
Haemophilus influenzae
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.00008
-
D-arabinose 5-phosphate
wild-type, pH 7.2, 25C
Haemophilus influenzae
0.0001
-
D-xylulose 5-phosphate
wild-type, pH 7.2, 25C
Haemophilus influenzae
0.0002
-
D-ribose 5-phosphate
wild-type, pH 7.2, 25C
Haemophilus influenzae
0.0002
-
D-ribulose 5-phosphate
mutant K386A, pH 7.2, 25C
Haemophilus influenzae
0.0003
-
D-ribulose
wild-type, pH 7.2, 25C
Haemophilus influenzae
0.0008
-
NADPH
mutant K386A, pH 7.2, 25C
Haemophilus influenzae
0.0013
-
(2R,3R)-2,3-dihydroxy-4-oxobutyl-phosphate
wild-type, pH 7.2, 25C
Haemophilus influenzae
0.0025
-
D-ribulose 5-phosphate
mutant R18A, pH 7.2, 25C
Haemophilus influenzae
0.029
-
D-ribulose 5-phosphate
wild-type, pH 7.2, 25C
Haemophilus influenzae
0.04
-
NADPH
mutant R18A, pH 7.2, 25C
Haemophilus influenzae
0.05
-
NADPH
wild-type, pH 7.2, 25C
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
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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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1
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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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7
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12
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7
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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
1
3
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1
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1
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3
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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