EC Number | Cloned (Comment) | Organism |
---|---|---|
2.7.1.100 | gene mtnK, encoded in the mtnKA operon | Bacillus subtilis |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.7.1.100 | additional information | - |
additional information | the Km for ribose is 80times higher than for S-methyl-5-thio-D-ribose | Bacillus subtilis | |
2.7.1.100 | 0.06 | - |
S-methyl-5-thio-D-ribose | pH 8.0, 25°C | Bacillus subtilis | |
2.7.1.100 | 4.8 | - |
D-ribose | pH 8.0, 25°C | Bacillus subtilis |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
2.7.1.100 | Mg2+ | required | Bacillus subtilis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.1.100 | ATP + S-methyl-5-thio-D-ribose | Bacillus subtilis | physiological substrate | ADP + S-methyl-5-thio-alpha-D-ribose 1-phosphate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.7.1.100 | Bacillus subtilis | - |
gene mtnK | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.1.100 | ATP + D-ribose | - |
Bacillus subtilis | ADP + D-ribose 1-phosphate | - |
? | |
2.7.1.100 | ATP + S-methyl-5-thio-D-ribose | best substrate | Bacillus subtilis | ADP + S-methyl-5-thio-alpha-D-ribose 1-phosphate | - |
? | |
2.7.1.100 | ATP + S-methyl-5-thio-D-ribose | physiological substrate | Bacillus subtilis | ADP + S-methyl-5-thio-alpha-D-ribose 1-phosphate | - |
? | |
2.7.1.100 | additional information | 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 | Bacillus subtilis | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.7.1.100 | MtnK | - |
Bacillus subtilis |
2.7.1.100 | MTR kinase | - |
Bacillus subtilis |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.7.1.100 | 25 | 35 | ribose kinase activity | Bacillus subtilis |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.7.1.100 | 7 | 8.5 | ribose kinase activity | Bacillus subtilis |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
2.7.1.100 | ATP | - |
Bacillus subtilis |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.7.1.100 | 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 | Bacillus subtilis |
2.7.1.100 | metabolism | the enzyme catalyze the first reaction of a ribose metabolic pathway, overview | Bacillus subtilis |