Information on EC 2.7.1.16 - ribulokinase

for references in articles please use BRENDA:EC2.7.1.16
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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.7.1.16
-
RECOMMENDED NAME
GeneOntology No.
ribulokinase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + L(or D)-ribulose = ADP + L(or D)-ribulose 5-phosphate
show the reaction diagram
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-arabinose degradation I
-
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degradation of pentoses
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Pentose and glucuronate interconversions
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
ATP:L(or D)-ribulose 5-phosphotransferase
Ribitol and L-arabinitol can also act as acceptors.
CAS REGISTRY NUMBER
COMMENTARY hide
9030-57-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
mutant araA-2
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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inactivation of the araK gene severely impairs the growth on arabinose
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + D-ribulose
ADP + D-ribulose 5-phosphate
show the reaction diagram
ATP + L-ribulose
ADP + L-ribulose 5-phosphate
show the reaction diagram
D-ribitol + ATP
D-ribitol 5-phosphate + ADP
show the reaction diagram
-
-
-
-
?
D-xylulose + ATP
D-xylose 5-phosphate + ADP
show the reaction diagram
D-xylulose + ATP
D-xylulose 5-phosphate + ADP
show the reaction diagram
L-arabitol + ATP
L-arabitol 5-phosphate + ADP
show the reaction diagram
L-xylulose + ATP
L-xylose 5-phosphate + ADP
show the reaction diagram
L-xylulose + ATP
L-xylulose 5-phosphate + ADP
show the reaction diagram
additional information
?
-
-
the enzyme is incapable of phosphorylating D-xylulose, D-glucose, D-fructose, and D-ribose
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + D-ribulose
ADP + D-ribulose 5-phosphate
show the reaction diagram
ATP + L-ribulose
ADP + L-ribulose 5-phosphate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
beta,gamma-imidoadenosine 5'-triphosphate
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competitive inhibition to MgATP2- and uncompetitive to L-ribulose
L-erythrulose
p-chloromercuribenzoate
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-
additional information
not inhibitory or activating: K+,Li+, Ca2+, and EDTA
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
20 mM, increases ribulokinase activity up to 175%
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02 - 7
ATP
5.5
D-ribitol
-
22°C, pH 7.5
0.27 - 0.94
D-ribulose
16
D-xylulose
-
22°C, pH 7.5
4
L-arabitol
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22°C, pH 7.5
0.111 - 0.96
L-ribulose
3.4
L-xylulose
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22°C, pH 7.5
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.84
ATP
-
22°C, pH 7.5, without any sugar
109
D-ribitol
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22°C, pH 7.5
74
D-ribulose
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22°C, pH 7.5
33
D-xylulose
-
22°C, pH 7.5
64
L-arabitol
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22°C, pH 7.5
41 - 80
L-ribulose
70
L-xylulose
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22°C, pH 7.5
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7.7
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about half-maximal activity at pH 6 and pH 7.7
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
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room temperature, assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
Q9KBQ3
Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125);
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
61000
x * 61000, SDS-PAGE
96500 - 100000
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osmotic pressure measurement, ultracentrifugation, ultracentrifugation and diffusion method
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in complex with L-ribulose, vapor diffusion method, using 30% (w/v) PEG4000, 0.2 M sodium acetate, 0.1 M Tris, pH 8.5
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
unstable below
641011
7.6
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and above, stable at least 30 min at 60.5°C
641010
10
30 min, 70% residual activity
739743
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
30 min, at least 90% residual activity
60.5
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at least 30 min stable at pH 7.6
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dilute enzyme solutions are highly unstable
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GSH stabilizes, but does not reactivate
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
deeply frozen, several months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA affinity column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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expressed in Escherichia coli BL21(DE3)-codon+RIL cells
expression in Corynebacterium glutamicum. Corynebacterium glutamicum is metabolically engineered to broaden its substrate utilization range to include L-arabinose. The resultant CRA1 recombinant strain expressed the Escherichia coli genes araA, araB, and araD encoding L-arabinose isomerase, L-ribulokinase, and L-ribulose-5-phosphate 4-epimerase, respectively, under the control of a constitutive promoter. Unlike the wild-type strain, CRA1 is able to grow on mineral salts medium containing L-arabinose as the sole carbon and energy source. The three cloned genes are expressed to the same levels whether cells are cultured in the presence of D-glucose or L-arabinose. Strain CRA1 is able to utilize L-arabinose as a substrate for organic acid production even in the presence of D-glucose
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expression in Escherichia coli
expression in Saccharomyces cerevisiae. Improvement of a bacterial L-arabinose utilization pathway consisting of L-arabinose isomerase from Bacillus subtilis and L-ribulokinase and L-ribulose-5-phosphate 4-epimerase from Escherichia coli after expression of the corresponding genes in Saccharomyces cerevisiae. These improvements make up a new starting point for the construction of more-efficient industrial L-arabinose-fermenting yeast strains by evolutionary engineering
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
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improvement of a bacterial L-arabinose utilization pathway consisting of L-arabinose isomerase from Bacillus subtilis and L-ribulokinase and L-ribulose-5-phosphate 4-epimerase from Escherichia coli after expression of the corresponding genes in Saccharomyces cerevisiae. These improvements make up a new starting point for the construction of more-efficient industrial L-arabinose-fermenting yeast strains by evolutionary engineering
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