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Literature summary extracted from

  • Cicchillo, R.M.; Zhang, H.; Blodgett, J.A.; Whitteck, J.T.; Li, G.; Nair, S.K.; van der Donk, W.A.; Metcalf, W.W.
    An unusual carbon-carbon bond cleavage reaction during phosphinothricin biosynthesis (2009), Nature, 459, 871-874.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.13.11.72 expression in Escherichia coli Streptomyces viridochromogenes

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.13.11.72 to 1.8 A resolution. The overall structure consists of imperfect tandem repeats of a bi-domain architecture. Each of the repeats is composed of an all-alpha-helical domain linked to a beta-barrel fold characteristic of the cupin superfamily. A Cd(II) ion is situated at the base of the active site and is coordinated by residues His 129, Glu 176 and His 182 Streptomyces viridochromogenes

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.13.11.72 Iron mononuclear non-haem iron(II)-dependent enzyme Streptomyces viridochromogenes

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.72 Streptomyces viridochromogenes Q5IW40
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.11.72 2-hydroxyethylphosphonate + O2
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 Streptomyces viridochromogenes hydroxymethylphosphonate + formate all four electrons required for reduction of O2 are provided by the substrate. Occurence of an intermediate species in which oxygen derived from O2 exchanges with water ?

Cofactor

EC Number Cofactor Comment Organism Structure
1.13.11.72 additional information no cofactors required Streptomyces viridochromogenes