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Literature summary for 4.7.1.1 extracted from

  • Kamat, S.S.; Williams, H.J.; Raushel, F.M.
    Intermediates in the transformation of phosphonates to phosphate by bacteria (2011), Nature, 480, 570-573.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.7.1.1

Metals/Ions

Metals/Ions Comment Organism Structure
Iron enzyme binds 2.2 equivalents of iron per monomer Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli P16688
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alpha-D-ribose 1-methylphosphonate 5-phosphate the carbon-phosphorus bond of the substrate is cleaved via a radical-based reaction to alpha-D-ribose 1,2-cyclic-phosphate 5-phosphate and methane in the presence of S-adenosyl-L-methionine. Enzyme additionally requires S-adenosyl-L-methionine Escherichia coli alpha-D-ribose 1,2-cyclic-phosphate 5-phosphate + methane
-
 ?

Synonyms

Synonyms Comment Organism
phnJ
-
 Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.8
-
 assay at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine
-
 Escherichia coli
[4Fe-4S]-center enzyme shows a absorption band centered at 403 nm and has a reddish-brown colour. The absorption band disappears upon addition of 1 mM dithionite Escherichia coli

General Information

General Information Comment Organism
physiological function deletion of the enzyme gene from Escherichia coli leads to the detection of alpha-D-ribose 1-methylphosphonate in the growth medium. alpha-D-Ribose 1-methylphosphonate is the ultimate substrate for the actual C-P lyase reaction Escherichia coli