Information on EC 2.7.1.16 - ribulokinase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.7.1.16
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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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Metabolic pathways
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Pentose and glucuronate interconversions
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degradation of pentoses
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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
strain bB/r, mutant araA-2
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-
Manually annotated by BRENDA team
strain 124-2
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Manually annotated by BRENDA team
strain 124-2
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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
?
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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
-
22C, pH 7.5
0.27 - 0.94
D-ribulose
16
D-xylulose
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22C, pH 7.5
4
L-arabitol
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22C, pH 7.5
0.111 - 0.96
L-ribulose
3.4
L-xylulose
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22C, pH 7.5
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.84
ATP
Escherichia coli
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22C, pH 7.5, without any sugar
109
D-ribitol
Escherichia coli
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22C, pH 7.5
74
D-ribulose
Escherichia coli
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22C, pH 7.5
33
D-xylulose
Escherichia coli
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22C, pH 7.5
64
L-arabitol
Escherichia coli
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22C, pH 7.5
41 - 80
L-ribulose
70
L-xylulose
Escherichia coli
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22C, 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
ORGANISM
UNIPROT
Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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unstable below
641011
7.6
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and above, stable at least 30 min at 60.5C
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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