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Information on EC 2.7.8.37 - alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase for references in articles please use BRENDA:EC2.7.8.37
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EC Tree
The enzyme appears in viruses and cellular organisms
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PhnI
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in the presence of PhnG, PhnH and PhnL
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ATP + methylphosphonate = alpha-D-ribose 1-methylphosphonate 5-triphosphate + adenine
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ATP:methylphosphonate 5-triphosphoribosyltransferase
Isolated from the bacterium Escherichia coli.
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ATP + H2O
adenine + D-ribose-5-triphosphate
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ATP + methylphosphonate
adenine + alpha-D-ribose-1-methylphosphonate-5-triphosphate
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GTP + H2O
guanine + D-ribose-5-triphosphate
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13
ATP
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PhnI, nucleosidase activity, pH not specified in the publication, temperature not specified in the publication
350
ATP
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PhnI, PhnG, PhnH and PhnL, GST tags in situ removed, proteins begin to precipitate after removal of the GST tags, therefore kinetic constants are not definitive, pH not specified in the publication, temperature not specified in the publication
83
GTP
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PhnI, nucleosidase activity, pH not specified in the publication, temperature not specified in the publication
340
GTP
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PhnI, PhnG, PhnH and PhnL, GST tags in situ removed, proteins begin to precipitate after removal of the GST tags, therefore kinetic constants are not definitive, pH not specified in the publication, temperature not specified in the publication
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brenda
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Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
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GST fusion proteins: GSTrap column, His-tagged proteins: HisTrap column
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GST fusion proteins of PhnI and PhnL expressed in Escherichia coli BL21(DE3), His-tagged PhnG and PhnH expressed in Escherichia coli BL21(DE3)
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Kamat, S.S.; Williams, H.J.; Raushel, F.M.
Intermediates in the transformation of phosphonates to phosphate by bacteria
Nature
480
570-573
2011
Escherichia coli
brenda
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2.7.8.37 alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase
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