Literature summary for 1.13.11.72 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.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Streptomyces viridochromogenes

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

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

Organism

Organism	UniProt	Comment	Textmining
Streptomyces viridochromogenes	Q5IW40	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2-hydroxyethylphosphonate + O2	-	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

Cofactor	Comment	Organism	Structure
additional information	no cofactors required	Streptomyces viridochromogenes

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Release 2023.1 (January 2023)