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Information on EC 2.7.1.15 - ribokinase
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2.7.1.15 ribokinaseIUBMB Comments
2-Deoxy-D-ribose can also act as acceptor.
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Word Map
- 2.7.1.15
-
adp-dependent
- fructokinase
- glucokinases
- phosphopentomutase
- phosphofructokinase-2
-
fructose-6-p
-
ribose-binding
- diagnostics
The enzyme appears in viruses and cellular organisms
Synonyms
ribokinase, sa239, d-ribokinase, rv2436, ms4585, at1g17160, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D-ribokinase
deoxyribokinase
-
-
-
-
rbsK1
ribokinase
ribokinase (phosphorylating)
-
-
-
-
Sa239
D-ribokinase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + D-ribose = ADP + D-ribose 5-phosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
phospho group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
ATP:D-ribose 5-phosphotransferase
2-Deoxy-D-ribose can also act as acceptor.
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CAS REGISTRY NUMBER
COMMENTARY
9026-84-0
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 2-deoxy-D-ribitol
ADP + 2-deoxy-D-ribitol 5-phosphate
-
41% of the activity with 2-deoxy-D-ribose
-
-
?
dATP + D-ribose
dADP + D-ribose 5-phosphate
-
108% of the activity with ATP
-
-
?
dCTP + D-ribose
dCDP + D-ribose 5-phosphate
-
25% of the activity with ATP
-
-
?
dGTP + D-ribose
dGDP + D-ribose 5-phosphate
-
50% of the activity with ATP
-
-
?
GTP + D-ribose
GDP + D-ribose 5-phosphate
-
32% of the activity with ATP
-
-
?
ITP + D-ribose
IDP + D-ribose 5-phosphate
-
37% of the activity with ATP
-
-
?
ATP + 2-deoxy-D-ribose
ADP + 2-deoxy-D-ribose 5-phosphate
-
75% of the activity with D-ribose
-
-
?
ATP + 2-deoxy-D-ribose
ADP + 2-deoxy-D-ribose 5-phosphate
31% if the activity with D-ribose
-
-
?
ATP + 2-deoxy-D-ribose
ADP + 2-deoxy-D-ribose 5-phosphate
-
-
-
?
ATP + 2-deoxy-D-ribose
ADP + 2-deoxy-D-ribose 5-phosphate
-
-
-
-
?
ATP + 2-deoxy-D-ribose
ADP + 2-deoxy-D-ribose 5-phosphate
-
first step in the inducible fermentation pathway for this sugar
-
?
ATP + D-arabinose
ADP + D-arabinose 5-phosphate
0.74% if the activity with D-ribose
-
-
?
ATP + D-arabinose
ADP + D-arabinose 5-phosphate
-
4% if the activity with D-ribose
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
-
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
-
-
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
-
highly specific for ribose phosphorylation
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
the enzyme catalyzes the first step of ribose metabolism
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
the enzyme catalyzes the first step of ribose metabolism
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
-
-
-
-
?
CTP + D-ribose
CDP + D-ribose 5-phosphate
-
18% of the activity with ATP
-
-
?
additional information
?
-
-
mutation of a gene encoding a putative ribokinase leads to reduced salt tolerance under potassium limitation in Bacillus subtilis
-
-
?
additional information
?
-
-
L-ribose and L-arabinose are not substrates for the recombinant enzyme
-
-
?
additional information
?
-
GTP displays activity, but at a level which was two orders of magnitude lower versus ATP
-
-
?
additional information
?
-
-
no significant phosphorylation of D-fructose, D-galactose and D-xylose
-
-
?
additional information
?
-
-
mycobacterial topoisomerase I (TopA) is found to physically interact with ribokinase both in vitro and in vivo. The interaction between ribokinase and topoisomerase I has opposite effects on their respective function. While the interaction between the two proteins inhibits the ability of topoisomerase I to relax supercoiled DNA, it stimulates ribokinase activity
-
-
?
additional information
?
-
-
mycobacterial topoisomerase I (TopA) is found to physically interact with ribokinase both in vitro and in vivo. The interaction between ribokinase and TopA has opposite effects on their respective function. While the interaction between the two proteins inhibits the ability of TopA to relax supercoiled DNA, it stimulates ribokinase activity
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 2-deoxy-D-ribose
ADP + 2-deoxy-D-ribose 5-phosphate
-
-
-
?
ATP + 2-deoxy-D-ribose
ADP + 2-deoxy-D-ribose 5-phosphate
-
first step in the inducible fermentation pathway for this sugar
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
-
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
the enzyme catalyzes the first step of ribose metabolism
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
the enzyme catalyzes the first step of ribose metabolism
-
-
?
additional information
?
-
-
mutation of a gene encoding a putative ribokinase leads to reduced salt tolerance under potassium limitation in Bacillus subtilis
-
-
?
additional information
?
-
-
mycobacterial topoisomerase I (TopA) is found to physically interact with ribokinase both in vitro and in vivo. The interaction between ribokinase and topoisomerase I has opposite effects on their respective function. While the interaction between the two proteins inhibits the ability of topoisomerase I to relax supercoiled DNA, it stimulates ribokinase activity
-
-
?
additional information
?
-
-
mycobacterial topoisomerase I (TopA) is found to physically interact with ribokinase both in vitro and in vivo. The interaction between ribokinase and TopA has opposite effects on their respective function. While the interaction between the two proteins inhibits the ability of TopA to relax supercoiled DNA, it stimulates ribokinase activity
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cd2+
Co2+
Cs+
Cu2+
-
can replace Mg2+ in activation, optimal concentration: 10 mM, 20% of the activity with Mg2+
K+
Mg2+
Mn2+
NH4+
Ni2+
Zn2+
-
can replace Mg2+ in activation, optimal concentration: 1 mM, 27% of the activity with Mg2+
additional information
Cd2+
-
can replace Mg2+ in activation, optimal concentration: 5 mM, 68% of the activity with Mg2+
Co2+
the enzyme is dependent on monovalent as well as divalent cations for its catalytic activity. When magnesium is substituted with Co2+ and Mn2+ in the reaction mixture, the ribokinase activity got reduced to 60% and 45% as compared to that with Mg2+
Co2+
-
can replace Mg2+ in activation, optimal concentration: 5 mM, 87% of the activity with Mg2+
Cs+
-
activity is strongly dependent on the presence of monovalent cations in the order of decreasing efficiency: K+, NH4+, Cs+
Cs+
-
optimal activity obtained in presence of 0.5 M NH4+ or Cs+
K+
-
activity is strongly dependent on the presence of monovalent cations in the order of decreasing efficiency: K+, NH4+, Cs+
K+
the enzyme is dependent on monovalent as well as divalent cations for its catalytic activity. Among the monovalent cations, K+ shows highest activating effect. The activity drops to 90% and 45% with Cs+ and Na+, respectively, in comparison to K+
K+
monovalent ions such as K+ are able to enhance substrate affinity of Sa239 and activate the reaction catalyzed by Sa239
Mg2+
-
absolute requirement, optimal ratio of Mg2+ to ATP is 1.5 : 1, higher concentrations inhibit
Mg2+
the enzyme is dependent on monovalent as well as divalent cations for its catalytic activity. When magnesium is substituted with Co2+ and Mn2+ in the reaction mixture, the ribokinase activity got reduced to 60% and 45% as compared to that with Mg2+
Mg2+
-
absolute requirement for divalent cations, best satisfied by Mg2+
Mg2+
-
the change in the ratio from Mg2+ to ATP from 1 : 1 to 2 : 1 gives optimal activity
Mg2+
-
the catalytic reactivity of ribokinase is activated by the divalent cation Mg2+, in the absence of these metal ions, ribokinase loses its catalytic ability
Mn2+
-
cannot replace Mg2+ in the kinase reaction, 50 mM inhibit
Mn2+
the enzyme is dependent on monovalent as well as divalent cations for its catalytic activity. When magnesium is substituted with Co2+ and Mn2+ in the reaction mixture, the ribokinase activity got reduced to 60% and 45% as compared to that with Mg2+
Mn2+
-
can replace Mg2+ in activation
Mn2+
-
optimal concentration 5 mM, 61% of the activity with Mg2+
NH4+
-
activity is strongly dependent on the presence of monovalent cations in the order of decreasing efficiency: K+, NH4+, Cs+
NH4+
-
optimal activity obtained in presence of 0.5 M NH4+ or Cs+
Ni2+
-
can replace Mg2+, optimal concentration: 25-30 mM, 31% of the activity with Mg2+
additional information
no activity in the absence of divalent metal ions
additional information
-
no activity in the absence of divalent metal ions
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Mg2+
-
absolute requirement, optimal ratio of Mg2+ to ATP is 1.5 : 1, higher concentrations inhibit
additional information
-
2-deoxyribose-5-phosphate and ADP at concentrations up to 5.4 and 10 mM do not inhibit the reaction with nonsaturating levels of substrates
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
MtbTopA
-
when increasing amounts of Mycobacterium smegmatis topoisomerase I are mixed together with ribokinase, the amount of phosphorylated D-ribose products steadily increases, indicating that Mycobacterium smegmatis topoisomerase I stimulates the kinase activity of ribokinase
-
topoisomerase I
-
when increasing amounts of MsTopA are mixed together with ribokinase, the amount of phosphorylated D-ribose products steadily increases, indicating that topoisomerase I stimulates the kinase activity of Ms4585
-
phosphate
-
increases catalytic activity. KM-for ribose and ATP decreases in a concentration-dependent manner
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Liver Neoplasms, Experimental
Altered expression of ribokinase activity in Novikoff hepatoma variants.
Liver Neoplasms, Experimental
Multiple genetic changes determine ribose utilization by Novikoff hepatoma cell variants.
Tuberculosis
Physical and functional interaction between d-ribokinase and topoisomerase I has opposite effects on their respective activity in Mycobacterium smegmatis and Mycobacterium tuberculosis.
Tuberculosis
Ribokinase screened from T7 phage displayed Mycobacterium tuberculosis genomic DNA library had good potential for the serodiagnosis of tuberculosis.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
33.3
2-deoxy-D-ribitol
-
25°C, pH 7.5
0.15
D-ribose
pH 8.0, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE