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Information on EC 2.7.1.100 - S-methyl-5-thioribose kinase
for references in articles please use BRENDA:EC2.7.1.100
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EC Tree 2 Transferases
2.7 Transferring phosphorus-containing groups
2.7.1 Phosphotransferases with an alcohol group as acceptor
2.7.1.100 S-methyl-5-thioribose kinase
IUBMB Comments
CTP also acts, but more slowly.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
- 2.7.1.100
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salvage
- mta
- nucleosidase
- s-adenosylmethionine
-
klebsiella
- 5'-methylthioadenosine
- polyamine
-
mill
- mtr-1-p
- methylthioadenosine
- americana
-
nanomoles
- avocado
- aminoethoxyvinylglycine
-
bilobal
-
difluoride
-
kinase-containing
-
riscoe
- 5'-deoxy-5'-methylthioadenosine
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antiprotozoal
- esculentum
- persea
- aerogenes
- trifluoromethionine
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phosphotransferases
-
ferro
- medicine
Reaction Schemes
showSynonyms
mtr kinase, 5-methylthioribose kinase, methylthioribose kinase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5-methylthioribose kinase
ATP:S-methylthioribose kinase
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-
-
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kinase, 5-methylthioribose (phosphorylating)
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methylthioribose kinase
MTK
MTK1
MTR kinase
methylthioribose kinase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + S-methyl-5-thio-D-ribose = ADP + S-methyl-5-thio-alpha-D-ribose 1-phosphate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
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-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
5'-deoxyadenosine degradation II, S-methyl-5'-thioadenosine degradation I
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SYSTEMATIC NAME
IUBMB Comments
ATP:S-methyl-5-thio-D-ribose 1-phosphotransferase
CTP also acts, but more slowly.
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CAS REGISTRY NUMBER
COMMENTARY
68247-56-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alphaATP + 5-methylthioribose
alphaADP + 5-methylthioribose 1-phosphate
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Substrates: -
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ATP + 5-butylthioribose
ADP + 5-butylthioribose 1-phosphate
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Substrates: -
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ATP + 5-ethylthioribose
ADP + 5-ethylthioribose 1-phosphate
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Substrates: -
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ATP + 5-isopropylthioribose
ADP + 5-isopropylthioribose 1-phosphate
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Substrates: -
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ATP + 5-propylthioribose
ADP + 5-propylthioribose 1-phosphate
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Substrates: -
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CTP + 5-methylthioribose
CDP + 5-methylthioribose 1-phosphate
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Substrates: 20% of activity with ATP
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dATP + 5-methylthioribose
dADP + 5-methylthioribose 1-phosphate
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Substrates: 120% of activity with ATP
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ATP + 5-isobutylthioribose
ADP + 5-isobutylthioribose 1-phosphate
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Substrates: -
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ATP + 5-isobutylthioribose
ADP + 5-isobutylthioribose 1-phosphate
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Substrates: -
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ATP + 5-methylthioribose
ADP + 5-methylthioribose 1-phosphate
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Substrates: -
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ATP + 5-methylthioribose
ADP + 5-methylthioribose 1-phosphate
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Substrates: no activity with GTP and UTP
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ATP + 5-methylthioribose
ADP + 5-methylthioribose 1-phosphate
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Substrates: may be a primary enzyme involved in the recycling of the methylthio group of 5-methylthioribose back into methionine
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ATP + 5-methylthioribose
ADP + 5-methylthioribose 1-phosphate
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Substrates: -
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ATP + 5-methylthioribose
ADP + 5-methylthioribose 1-phosphate
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Substrates: key step in recycling of methionine from 5'-methylthioadenosine a co-product of polyamine biosynthesis, expression of methylthioribose kinase may be under control of the methionine regulon
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ATP + 5-methylthioribose
ADP + 5-methylthioribose 1-phosphate
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Substrates: no activity with AMP, ADP and alpha,beta-CH2-ATP
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ATP + 5-methylthioribose
ADP + 5-methylthioribose 1-phosphate
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Substrates: enzyme may be involved in an alternative pathway of methionine synthesis in plant tissues
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ATP + 5-methylthioribose
ADP + 5-methylthioribose 1-phosphate
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Substrates: -
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ATP + 5-methylthioribose
ADP + 5-methylthioribose 1-phosphate
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Substrates: -
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ATP + 5-methylthioribose
ADP + 5-methylthioribose 1-phosphate
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Substrates: -
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ATP + 5-methylthioribose
ADP + 5-methylthioribose 1-phosphate
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Substrates: -
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ATP + S-methyl-5-thio-D-ribose
ADP + 5-methyl-5-thio-D-ribose 1-phosphate
Substrates: -
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ATP + S-methyl-5-thio-D-ribose
ADP + 5-methyl-5-thio-D-ribose 1-phosphate
Substrates: structure analysis in Arabidopsis thaliana, provides template for structure-based design of agrochemicals, particularly herbicides with the possibility that effectiveness can be regulated by nutrient levels
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ATP + S-methyl-5-thio-D-ribose
ADP + S-methyl-5-thio-alpha-D-ribose 1-phosphate
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Substrates: best substrate
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ATP + S-methyl-5-thio-D-ribose
ADP + S-methyl-5-thio-alpha-D-ribose 1-phosphate
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Substrates: physiological substrate
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ATP + S-methyl-5-thio-D-ribose
ADP + S-methyl-5-thio-D-ribose 1-phosphate
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Substrates: -
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ATP + S-methyl-5-thio-D-ribose
ADP + S-methyl-5-thio-D-ribose 1-phosphate
Substrates: -
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ATP + S-methyl-5-thio-D-ribose
ADP + S-methyl-5-thio-D-ribose 1-phosphate
Substrates: enzyme is involved in the recycling of methionine through the methylthioadenosine, i.e. MTA, cycle
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ATP + S-methyl-5-thio-D-ribose
ADP + S-methyl-5-thio-D-ribose 1-phosphate
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Substrates: -
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ATP + S-methyl-5-thio-D-ribose
ADP + S-methyl-5-thio-D-ribose 1-phosphate
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Substrates: 5-methylthioribose kinase is a key enzyme in methionine salvage in bacteria
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ATP + S-methyl-5-thio-D-ribose
ADP + S-methyl-5-thio-D-ribose 1-phosphate
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Substrates: dissociative mechanism
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ATP + S-methyl-5-thio-D-ribose
ADP + S-methyl-5-thio-D-ribose 1-phosphate
Substrates: -
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ATP + S-methyl-5-thio-D-ribose
ADP + S-methyl-5-thio-D-ribose 1-phosphate
Substrates: enzyme is involved in the recycling of methionine through the methylthioadenosine, i.e. MTA, cycle
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additional information
?
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Substrates: the enzyme has significant ribose kinase activity, it has a hydrophobic pocket that specifically recognizes the methylthio group of the substrate. MTK shows a 9fold higher Vmax for ribose kinase activity than for S-methyl-5-thio-D-ribose kinase activity, but also has a several fold higher Km for ribose
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additional information
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Substrates: the enzyme regulation is related to the sulfur metabolism
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additional information
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Substrates: the enzyme regulation is related to the sulfur metabolism
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + S-methyl-5-thio-D-ribose
ADP + 5-methyl-5-thio-D-ribose 1-phosphate
Substrates: -
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ATP + S-methyl-5-thio-D-ribose
ADP + S-methyl-5-thio-alpha-D-ribose 1-phosphate
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Substrates: physiological substrate
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ATP + 5-methylthioribose
ADP + 5-methylthioribose 1-phosphate
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Substrates: -
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ATP + 5-methylthioribose
ADP + 5-methylthioribose 1-phosphate
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Substrates: may be a primary enzyme involved in the recycling of the methylthio group of 5-methylthioribose back into methionine
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ATP + 5-methylthioribose
ADP + 5-methylthioribose 1-phosphate
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Substrates: -
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ATP + 5-methylthioribose
ADP + 5-methylthioribose 1-phosphate
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Substrates: key step in recycling of methionine from 5'-methylthioadenosine a co-product of polyamine biosynthesis, expression of methylthioribose kinase may be under control of the methionine regulon
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ATP + 5-methylthioribose
ADP + 5-methylthioribose 1-phosphate
-
Substrates: enzyme may be involved in an alternative pathway of methionine synthesis in plant tissues
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ATP + 5-methylthioribose
ADP + 5-methylthioribose 1-phosphate
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Substrates: -
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ATP + 5-methylthioribose
ADP + 5-methylthioribose 1-phosphate
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Substrates: -
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ATP + 5-methylthioribose
ADP + 5-methylthioribose 1-phosphate
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Substrates: -
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ATP + 5-methylthioribose
ADP + 5-methylthioribose 1-phosphate
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Substrates: -
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ATP + S-methyl-5-thio-D-ribose
ADP + S-methyl-5-thio-D-ribose 1-phosphate
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Substrates: -
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ATP + S-methyl-5-thio-D-ribose
ADP + S-methyl-5-thio-D-ribose 1-phosphate
Substrates: enzyme is involved in the recycling of methionine through the methylthioadenosine, i.e. MTA, cycle
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ATP + S-methyl-5-thio-D-ribose
ADP + S-methyl-5-thio-D-ribose 1-phosphate
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Substrates: -
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ATP + S-methyl-5-thio-D-ribose
ADP + S-methyl-5-thio-D-ribose 1-phosphate
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Substrates: 5-methylthioribose kinase is a key enzyme in methionine salvage in bacteria
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ATP + S-methyl-5-thio-D-ribose
ADP + S-methyl-5-thio-D-ribose 1-phosphate
Substrates: enzyme is involved in the recycling of methionine through the methylthioadenosine, i.e. MTA, cycle
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additional information
?
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Substrates: the enzyme regulation is related to the sulfur metabolism
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additional information
?
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Substrates: the enzyme regulation is related to the sulfur metabolism
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ho3+
trivalent holmium ions can isomorphously replace Mg2+ form an ADP-2Ho complex in the nucleotide-binding domain of Bacillus subtilis 5-methylthioribose kinase The structure of ADP-2Ho reveals that the two Ho ions are approximately 4 A apart and are likely to share their ligands: the phosphoryl O atoms of ADP and a water molecule
Mg2+
Mn2+
Mg2+
-
divalent metal ion is strictely required for activity, Mg2+ is most effective
Mg2+
-
divalent metal ion is strictely required for activity, Mg2+ is most effective
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dithiothreitol
-
required for activity, maximal activity at 20 mM
dithiothreitol
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can partially be replaced by 20 mM 2-mercaptoethanol or glutathione
additional information
strong upregulation of enzyme expression during sulfur starvation
-
additional information
-
strong upregulation of enzyme expression during sulfur starvation
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Starvation
Transcriptional analysis between two wheat near-isogenic lines contrasting in aluminum tolerance under aluminum stress.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
the Km for ribose is 80times higher than for S-methyl-5-thio-D-ribose
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
mapping of secondary structural elements by in silico analysis, effect of pH on kinase activity, structure compared to enzyme structure of Bacilus subtilis, same protein kinase fold observed in other evolutionary related protein kinase-like phosphotransferases
additional information
-
mapping of secondary structural elements by in silico analysis, effect of pH on kinase activity, structure compared to enzyme structure of Bacilus subtilis, same protein kinase fold observed in other evolutionary related protein kinase-like phosphotransferases
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme expression is induced by sulfur, nitrogen or carbon starvation
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
strong upregulation of enzyme expression during sulfur starvation
brenda
expression of methylthioribose kinase and other enzymes of the yang cycle is phloem-specific
brenda
expression of methylthioribose kinase and other enzymes of the yang cycle is phloem-specific
brenda
strong upregulation of enzyme expression during sulfur starvation
brenda
both in Arabidopsis and in Plantago, the Yang cycle enzymes are encoded by highly vasculature-specific genes or by genes showing much stronger expression in the vasculature than in nonvascular tissue. There are high expression levels of S-adenosyl methionine decarboxylases in the vasculature of Arabidopsis and Plantago
brenda
both in Arabidopsis and in Plantago, the Yang cycle enzymes are encoded by highly vasculature-specific genes or by genes showing much stronger expression in the vasculature than in nonvascular tissue. There are significantly higher concentrations of Met, S-adenosyl methionine, and 5-methylthioadenosine and a less pronounced enrichment of polyamines in Plantago vascular versus nonvascular tissue and high expression levels of S-adenosyl methionine decarboxylases in the vasculature of Arabidopsis and Plantago
brenda
Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
although most bacteria, yeasts, and animals have the complete methionine salvage pathway, MSP enzymes, these organisms have 5-methylthioadenosine phosphorylase, MtnP, instead of MtnK
metabolism
additional information
metabolism
-
the enzyme catalyze the first reaction of a ribose metabolic pathway, overview
additional information
proteomic analysis of rice root proteins in untreated and in roots infected with Herbaspirillum seropedicae SmR1, overview. The 5-methylthioribose kinase is upregulated. RT-qPCR analysis also confirms that the methionine recycling and phytosiderophore biosynthesis genes are upregulated, while ACC oxidase mRNA level is down-regulated in rice roots colonized by bacteria
additional information
-
proteomic analysis of rice root proteins in untreated and in roots infected with Herbaspirillum seropedicae SmR1, overview. The 5-methylthioribose kinase is upregulated. RT-qPCR analysis also confirms that the methionine recycling and phytosiderophore biosynthesis genes are upregulated, while ACC oxidase mRNA level is down-regulated in rice roots colonized by bacteria
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50000
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