Information on EC 2.7.1.15 - ribokinase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
2.7.1.15
-
RECOMMENDED NAME
GeneOntology No.
ribokinase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ATP + D-ribose = ADP + D-ribose 5-phosphate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
phospho group transfer
-, Q8NQR0
-
phospho group transfer
Corynebacterium glutamicum KB1547
-
-
-
Phosphorylation
-
-
PATHWAY
KEGG Link
MetaCyc Link
Pentose phosphate pathway
-
ribose degradation
-
SYSTEMATIC NAME
IUBMB Comments
ATP:D-ribose 5-phosphotransferase
2-Deoxy-D-ribose can also act as acceptor.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D-ribokinase
-
-
-
-
deoxyribokinase
-
-
-
-
Ms4585
-
gene name
rbsK1
Corynebacterium glutamicum KB1547
Q8NQR0
-
-
ribokinase
Q8NQR0
-
ribokinase
Corynebacterium glutamicum KB1547
Q8NQR0
-
-
ribokinase
-
-
ribokinase
B8CWQ8
-
ribokinase
-
-
ribokinase (phosphorylating)
-
-
-
-
Rv2436
-
gene name
Sa239
-
gene name
Sa239
Q5HJA8
-
CAS REGISTRY NUMBER
COMMENTARY
9026-84-0
-
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-
ribokinase plays a key role in the recycling of sugars produced from the metabolism of nucleotides
physiological function
-
ribokinase inhibits the function of MsTopA in relaxing supercoiled DNA
physiological function
-
ribokinase inhibits the function of topoisomerase I in relaxing supercoiled DNA
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 2-deoxy-D-ribitol
ADP + 2-deoxy-D-ribitol 5-phosphate
show the reaction diagram
-
41% of the activity with 2-deoxy-D-ribose
-
-
?
ATP + 2-deoxy-D-ribose
ADP + 2-deoxy-D-ribose 5-phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2-deoxy-D-ribose
ADP + 2-deoxy-D-ribose 5-phosphate
show the reaction diagram
-
-
-
-
ATP + 2-deoxy-D-ribose
ADP + 2-deoxy-D-ribose 5-phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2-deoxy-D-ribose
ADP + 2-deoxy-D-ribose 5-phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2-deoxy-D-ribose
ADP + 2-deoxy-D-ribose 5-phosphate
show the reaction diagram
-
-
-
-
-
ATP + 2-deoxy-D-ribose
ADP + 2-deoxy-D-ribose 5-phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2-deoxy-D-ribose
ADP + 2-deoxy-D-ribose 5-phosphate
show the reaction diagram
-
first step in the inducible fermentation pathway for this sugar
-
?
ATP + 2-deoxy-D-ribose
ADP + 2-deoxy-D-ribose 5-phosphate
show the reaction diagram
-
31% if the activity with D-ribose
-
-
?
ATP + 2-deoxy-D-ribose
ADP + 2-deoxy-D-ribose 5-phosphate
show the reaction diagram
-
75% of the activity with D-ribose
-
-
?
ATP + D-arabinose
ADP + D-arabinose 5-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-arabinose
ADP + D-arabinose 5-phosphate
show the reaction diagram
-
0.74% if the activity with D-ribose
-
-
?
ATP + D-arabinose
ADP + D-arabinose 5-phosphate
show the reaction diagram
-
4% if the activity with D-ribose
-
-
?
ATP + D-arabinose
?
show the reaction diagram
-
weak activity
-
-
?
ATP + D-fructose
ADP + D-fructose 5-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
show the reaction diagram
-
-
-
-
-
ATP + D-ribose
ADP + D-ribose 5-phosphate
show the reaction diagram
P0A9J6
-
-
-
-
ATP + D-ribose
ADP + D-ribose 5-phosphate
show the reaction diagram
-
-
-
-
-
ATP + D-ribose
ADP + D-ribose 5-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
show the reaction diagram
-, Q8NQR0
-
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
show the reaction diagram
Q5HJA8
-
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
show the reaction diagram
-
highly specific for ribose phosphorylation
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
show the reaction diagram
Corynebacterium glutamicum KB1547
Q8NQR0
-
-
-
?
ATP + D-xylose
ADP + D-xylose 5-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-xylose
?
show the reaction diagram
-
1.06% if the activity with D-ribose
-
-
?
CTP + D-ribose
CDP + D-ribose 5-phosphate
show the reaction diagram
-
-
-
-
?
CTP + D-ribose
CDP + D-ribose 5-phosphate
show the reaction diagram
-
18% of the activity with ATP
-
-
?
dATP + D-ribose
dADP + D-ribose 5-phosphate
show the reaction diagram
-
108% of the activity with ATP
-
-
?
dCTP + D-ribose
dCDP + D-ribose 5-phosphate
show the reaction diagram
-
25% of the activity with ATP
-
-
?
dGTP + D-ribose
dGDP + D-ribose 5-phosphate
show the reaction diagram
-
50% of the activity with ATP
-
-
?
GTP + D-ribose
GDP + D-ribose 5-phosphate
show the reaction diagram
-
32% of the activity with ATP
-
-
?
ITP + D-ribose
IDP + D-ribose 5-phosphate
show the reaction diagram
-
37% 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
?
-
-
no significant phosphorylation of D-fructose, D-galactose and D-xylose
-
-
-
additional information
?
-
-
GTP displays activity, but at a level which was two orders of magnitude lower versus ATP
-
-
-
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
-
-
-
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + 2-deoxy-D-ribose
ADP + 2-deoxy-D-ribose 5-phosphate
show the reaction diagram
-
-
-
-
ATP + 2-deoxy-D-ribose
ADP + 2-deoxy-D-ribose 5-phosphate
show the reaction diagram
-
first step in the inducible fermentation pathway for this sugar
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
show the reaction diagram
-, Q8NQR0
-
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
show the reaction diagram
Corynebacterium glutamicum KB1547
Q8NQR0
-
-
-
?
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 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
-
-
-
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
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Cd2+
-
can replace Mg2+ in activation, optimal concentration: 5 mM, 68% of the activity with Mg2+
Co2+
-
-
Co2+
-
can replace Mg2+ in activation, optimal concentration: 5 mM, 87% of the activity with Mg2+
Cs+
-
optimal activity obtained in presence of 0.5 M NH4+ or Cs+
Cs+
-
Kd: 17 mM
Cs+
-
activity is strongly dependent on the presence of monovalent cations in the order of decreasing efficiency: K+, NH4+, Cs+
Cs+
-
activates
Cu2+
-
can replace Mg2+ in activation, optimal concentration: 10 mM, 20% of the activity with Mg2+
K+
-
Kd: 5mM
K+
-
activity is strongly dependent on the presence of monovalent cations in the order of decreasing efficiency: K+, NH4+, Cs+
K+
-
activates
K+
Q5HJA8
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+
-
absolute requirement for divalent cations, best satisfied by Mg2+
Mg2+
-
absolute requirement for divalent cations, best satisfied by Mg2+; the change in the ratio from Mg2+ to ATP from 1 : 1 to 2 : 1 gives optimal activity
Mg2+
-
optimum concentration at pH 6.2 of free Mg2+ is 2.5 mM
Mg2+
-
activity is cooperatively enhanced by Mn2+ and Mg2+
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+
-
can replace Mg2+ in activation
Mn2+
-
can replace Mg2+ in activation; optimal concentration 5 mM, 61% of the activity with Mg2+
NH4+
-
optimal activity obtained in presence of 0.5 M NH4+ or Cs+
NH4+
-
activity is strongly dependent on the presence of monovalent cations in the order of decreasing efficiency: K+, NH4+, Cs+
Ni2+
-
can replace Mg2+, optimal concentration: 25-30 mM, 31% of the activity with Mg2+
Zn2+
-
can replace Mg2+ in activation, optimal concentration: 1 mM, 27% of the activity with Mg2+
Mn2+
-
activity is cooperatively enhanced by Mn2+ and Mg2+
additional information
-
no activity in the absence of divalent metal ions
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-carboxyethylphosphonic acid
-
-
ATP
-
inhibition above 5 mM
ATP
-
substrate inhibition
D-arabinose
-
-
D-Erythrose
-
-
D-ribose
-
substrate inhibition
D-ribose 5-phosphate
-
inhibits the phosphorylation of D-ribose
Mg2+
-
absolute requirement, optimal ratio of Mg2+ to ATP is 1.5 : 1, higher concentrations inhibit
Mg2+
-
above 2.5 mM: gradual inhibition
N-(phosphonomethyl)-glycine
-
-
N-(phosphonomethyl)iminodiacetic acid
-
-
Na+
-
0.02 M, 30% inhibition
p-chloromercuribenzoate
-
-
Phosphonoacetic acid
-
-
Mn2+
-
50 mM inhibit
additional information
-
not: n-ethylmaleimide
-
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
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
-
NH4+
-
activates
phosphate
-
increases catalytic activity. KM-for ribose and ATP decreases in a concentration-dependent manner; marked dependency upon the presence of inorganic phosphate
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
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.035
-
2-deoxy-D-ribose
-
30C, pH 7
0.1
-
2-deoxy-D-ribose
-
30C, pH 7.4
1.8
-
2-deoxy-D-ribose
-
37C, pH 7.2
0.04
-
ATP
-
30C, pH 7, in presence of Mg2+
0.07
-
ATP
-
37C, pH 7.0, in presence of 5 mM phosphate
0.08
-
ATP
-
37C, pH 7.0, in presence of 2 mM phosphate
0.1
-
ATP
-
37C, pH 7.0, in presence of 1 mM phosphate
2.19
-
ATP
Q5HJA8
pH 8.0, 30C, 100 mM K+
4.66
-
ATP
Q5HJA8
pH 8.0, 30C, 0 mM K+
0.022
-
D-ribose
-
30C, pH 7
0.11
-
D-ribose
-
37C, pH 7.4, 20 mM phosphate
0.18
-
D-ribose
-
37C, pH 7.4
0.21
-
D-ribose
-
37C, pH 6.2, 20 mM phosphate
0.22
-
D-ribose
-
37C, pH 6.2, 20 mM arsenate
0.23
-
D-ribose
-
37C, pH 6.2, 5 mM phosphate
0.26
-
D-ribose
-
37C, pH 6.2, 5 mM arsenate
0.27
-
D-ribose
-
37C, pH 6.2, 1 mM phosphate
0.3
-
D-ribose
-
-
0.32
-
D-ribose
-
37C, pH 6.2, 1 mM arsenate
0.33
-
D-ribose
-
37C, pH 6.2, 20 mM vanadate
0.43
-
D-ribose
-
37C, pH 6.2, 0.5 mM phosphate or 5 mM vanadate
0.46
-
D-ribose
-
37C, pH 6.2, 1 mM vanadate
0.48
-
D-ribose
-
37C, pH 6.2, 0.5 mM arsenate
0.65
-
D-ribose
-
37C, pH 6.2
2
-
D-ribose
-
30C, pH 7.4
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
10.2
-
ATP
-
22C, pH 8.5
20.65
-
ATP
Q5HJA8
pH 8.0, 30C, 0 mM K+
47.81
-
ATP
Q5HJA8
pH 8.0, 30C, 100 mM K+
10.8
-
D-ribose
-
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
4.42
-
ATP
Q5HJA8
pH 8.0, 30C, 0 mM K+
22040
21.87
-
ATP
Q5HJA8
pH 8.0, 30C, 100 mM K+
22040
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.2
-
ATP
-
37C, pH 7.0, in presence of 1 mM phosphate
4.4
-
ATP
-
37C, pH 7.0, in presence of 2 mM phosphate
18.91
-
ATP
-
37C, pH 7.0, in presence of 5 mM phosphate
0.4
-
D-ribose 5-phosphate
-
22C, pH 8.5
0.4
-
D-ribose 5-phosphate
-
-
additional information
-
additional information
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
23.2
-
-
-
77
-
-
with D-ribose as substrate
89
-
-
with 2-deoxy-D-ribose as substrate
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.7
7.3
-
2-deoxy-D-ribose
7.1
7.8
-
-
8
-
Q5HJA8
assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
9
-
pH 5.5: about 45% of activity maximum, pH 9.0: about 55% of activity maximum
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
assay at
30
-
Q5HJA8
assay at
37
-
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578)
Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578)
Staphylococcus aureus (strain COL)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30800
-
-, Q8NQR0
predicted from the 307 amino acid sequence
33230
-
-
electrospray ionization mass spectrometry
62000
-
-
gel filtration
67800
-
-
high-speed sedimentation equilibrium method
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
Q5HJA8
crystal structure
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
20C or 16C, hanging drop method, 7 mg/ml protein mixed with an equal volume of mother liquor
-
4C, hanging drop vapour diffusion, Cs-bound ternary complex structure: P212121
-
ribokinase in complex with ribose and dinucleotide: there is one 33000 Da monomer of ribokinase in the asymmetric unit but the protein forms a dimer around a crystallographic twofold axis
-
several different types of crystals, apo ribokinase: space group P1 or P3x21, ATP ribokinase: tetragonal, ribose/AMP-PNP: P6x22
-
crystals are obtained using the sitting-drop method. Diffraction data are collected to a resolution of 3.1 A
B8CWQ8, -
by using the hanging-drop vapour-diffusion method, large crystals appear at 21.85C in conditions consisting of 23% PEG 3000, 0.1 M sodium citrate pH 5.6, the crystals diffract to 2.9 A resolution and belong to space group P6122 or P6522, with unit-cell parameters a=b=91.8 A, c=160.7 A
-
crystal structure of Sa239 in the absence of monovalent ions. The structure of Sa239 demonstrates that the C-terminal tail protrudes from the remaining part and interacts with the neighboring molecule, resulting in an dimerization form
Q5HJA8
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
60
-
-
5 min, complete inactivation
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-12C fraction IV retains 65% activity after two months
-
-10C gamma gel supernatants lose 64% activity in 3 months
-
-70C, in buffer/glycerol (1/1), the recombinant enzyme retains more than 50% of its activity after 1 year
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
using affinity chromatography
B8CWQ8, -
by affinity chromatography on a nickel-chelating column and gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
deletion mutant is expressed in Escherichia coli
-, Q8NQR0
expressed in the Escherichia coli ER2566 cells harboring the constructed expression plasmid encompassing the rbsK gene
-
overexpression in Escherichia coli
-
overexpressed in Escherichia coli as a His-tagged fusion protein
B8CWQ8, -
expression in Escherichia coli
-
overexpression in Escherichia coli
-
overexpression in Escherichia coli
-
expressed in Escherichia coli
Q5HJA8
the SUMO-Sa239 fusion protein is expressed in Escherichia coli BL21 (DE3) cells
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
the gene is a part of the uriR operon, gene expression is 36.6fold stimulated by D-ribose and 9.8fold stimulated by uridine when it is containing (30 mM) in the medium, deletion of the LacI/GalR-type regulator in the mutant strain KB1546 leads to enhanced expression
-, Q8NQR0
the gene is a part of the uriR operon, gene expression is 36.6fold stimulated by D-ribose and 9.8fold stimulated by uridine when it is containing (30 mM) in the medium, deletion of the LacI/GalR-type regulator in the mutant strain KB1546 leads to enhanced expression
Corynebacterium glutamicum KB1547
-
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
A13/103/116V
-
mutant shows no interaction with topoisomerase I. Mutant only partially retains its ability to inhibit the activity of topoisomerase I even at high protein concentrations. Topoisomerase I does not significantly stimulate the activity of the mutant protein
S11N/A14V
-
mutant shows no interaction with topoisomerase I. Mutant only partially retains its ability to inhibit the activity of topoisomerase I even at high protein concentrations. Topoisomerase I does not significantly stimulate the activity of the mutant protein
S11N/A14V
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mutant shows no interaction with topoisomerase I
M10N
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70 fold higher KM for deoxyribose but only 2 fold increased KM for ribose