Information on EC 3.6.1.63 - alpha-D-ribose 1-methylphosphonate 5-triphosphate diphosphatase

for references in articles please use BRENDA:EC3.6.1.63
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The expected taxonomic range for this enzyme is: Escherichia coli

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EC NUMBER
COMMENTARY hide
3.6.1.63
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RECOMMENDED NAME
GeneOntology No.
alpha-D-ribose 1-methylphosphonate 5-triphosphate diphosphatase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
alpha-D-ribose 1-methylphosphonate 5-triphosphate + H2O = alpha-D-ribose 1-methylphosphonate 5-phosphate + diphosphate
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
aminomethylphosphonate degradation
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glyphosate degradation III
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methylphosphonate degradation I
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methylphosphonate degradation II
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Phosphonate and phosphinate metabolism
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SYSTEMATIC NAME
IUBMB Comments
alpha-D-ribose-1-methylphosphonate-5-triphosphate diphosphohydrolase
Isolated from the bacterium Escherichia coli.
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
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LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-D-ribose 1-methylphosphonate 5-triphosphate + H2O
alpha-D-ribose 1-methylphosphonate 5-phosphate + diphosphate
show the reaction diagram
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-
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?
D-ribose 5-diphosphate + H2O
D-ribose 5-phosphate + phosphate
show the reaction diagram
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-
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?
D-ribose 5-triphosphate + H2O
D-ribose 5-phosphate + phosphate
show the reaction diagram
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-
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?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5
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assay at
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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membrane protein
Manually annotated by BRENDA team
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41700
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SDS-PAGE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloned into the pSPORT1 vector and expressed in Escherichia coli
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expressed in Escherichia coli
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Show AA Sequence (213 entries)
Please use the Sequence Search for a specific query.
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LINKS TO OTHER DATABASES (specific for EC-Number 3.6.1.63)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)