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EC Tree
The expected taxonomic range for this enzyme is: Bacteria, Archaea
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phnM
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alpha-D-ribose 1-methylphosphonate 5-triphosphate + H2O = alpha-D-ribose 1-methylphosphonate 5-phosphate + diphosphate
alpha-D-ribose 1-methylphosphonate 5-triphosphate + H2O = alpha-D-ribose 1-methylphosphonate 5-phosphate + diphosphate
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alpha-D-ribose 1-methylphosphonate 5-triphosphate + H2O = alpha-D-ribose 1-methylphosphonate 5-phosphate + diphosphate
when the hydrolysis reaction of D-ribose-5-triphosphate catalyzed by PhnM is conducted in oxygen-18 labeled water, the oxygen-18 is found exclusively in D-ribose-5-phosphate and not in diphosphate. Therefore, water attacks the alpha-phosphoryl group of D-ribose-5-triphosphate rather than the beta-phosphoryl group
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alpha-D-ribose-1-methylphosphonate-5-triphosphate diphosphohydrolase
Isolated from the bacterium Escherichia coli.
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alpha-D-ribose 1-methylphosphonate 5-triphosphate + H2O
alpha-D-ribose 1-methylphosphonate 5-phosphate + diphosphate
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D-ribose 5-diphosphate + H2O
D-ribose 5-phosphate + phosphate
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D-ribose 5-triphosphate + H2O
D-ribose 5-phosphate + phosphate
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110
alpha-D-ribose 1-methylphosphonate 5-triphosphate
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pH 8.5, temperature not specified in the publication
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brenda
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membrane protein
brenda
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malfunction
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in vivo complementation of the strains, in which phnC to phnP or phnH to phnP are deleted, with plasmids carrying various fragments of the phn operon reveal that the expression of phnC-phnP gene products is essential to restore growth on minimal medium with phosphonate as the sole phosphorus source, while phnG-phnM gene products are required for carbon-phosphorus lyase activity. The minimum size of the DNA required for the whole-cell carbon-phosphorus lyase activity is determined to be a 5.8-kb fragment, encompassing the phnG to phnM genes
physiological function
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nine gene products (PhnG, PhnH, PhnI, PhnJ, PhnK, PhnL, PhnM, PhnN, and PhnP) comprise a membrane-associated carbon-phosphorus lyase enzyme complex
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purified using gel filtration with a High Load Superdex 200 26/60 prep grade column followed by anion exchange chromatography
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cloned into the pSPORT1 vector and expressed in Escherichia coli
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expressed in Escherichia coli
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Yakovleva, G.M.; Kim, S.K.; Wanner, B.L.
Phosphate-independent expression of the carbon-phosphorus lyase activity of Escherichia coli
Appl. Microbiol. Biotechnol.
49
573-578
1998
Escherichia coli
brenda
Wanner, B.; Metcalf, W.
Molecular genetic studies of a 10.9-kb operon in Escherichia coli for phosphonate uptake and biodegradation
FEMS Microbiol. Lett.
100
133-139
1992
Escherichia coli
brenda
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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History
Enzyme Nomenclature
3.6.1.63 alpha-D-ribose 1-methylphosphonate 5-triphosphate diphosphatase
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