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Literature summary for 1.13.11.72 extracted from

  • Peck, S.C.; van der Donk, W.A.
    Go it alone four-electron oxidations by mononuclear non-heme iron enzymes (2017), J. Biol. Inorg. Chem., 22, 381-394 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.13.11.72

Crystallization (Commentary)

Crystallization (Comment) Organism
in vitro reconstitution of activity and determination of the crystal structure of Cd2+-substituted PhpD in complex with the 2-hydroxyethylphosphonate substrate Streptomyces viridochromogenes

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ a mononuclear non-heme iron-dependent enzyme Streptomyces viridochromogenes

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2-hydroxyethylphosphonate + O2 Streptomyces viridochromogenes
-
 hydroxymethylphosphonate + formate
-
 ir
2-hydroxyethylphosphonate + O2 Streptomyces viridochromogenes DSM 40736
-
 hydroxymethylphosphonate + formate
-
 ir

Organism

Organism UniProt Comment Textmining
Streptomyces viridochromogenes Q5IW40
-
-
Streptomyces viridochromogenes DSM 40736 Q5IW40
-
-

Reaction

Reaction Comment Organism Reaction ID
2-hydroxyethylphosphonate + O2 = hydroxymethylphosphonate + formate initial substrate oxidation by a ferric-superoxo-intermediate and a second oxidation by a ferryl species, catalytic mechanism, detailed overview Streptomyces viridochromogenes
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-hydroxyethylphosphonate + O2
-
 Streptomyces viridochromogenes hydroxymethylphosphonate + formate
-
 ir
2-hydroxyethylphosphonate + O2 an irreversible step involving O2 Streptomyces viridochromogenes hydroxymethylphosphonate + formate
-
 ir
2-hydroxyethylphosphonate + O2
-
 Streptomyces viridochromogenes DSM 40736 hydroxymethylphosphonate + formate
-
 ir
2-hydroxyethylphosphonate + O2 an irreversible step involving O2 Streptomyces viridochromogenes DSM 40736 hydroxymethylphosphonate + formate
-
 ir
additional information HEPD oxidizes a relatively unactivated substrate that cannot easily facilitate O2 activation. 2-Hydroxyethylphosphonate does not contain a thiol group that upon binding to the iron can activate it for catalysis, nor does it contain an 2-oxo acid functionality Streptomyces viridochromogenes ?
-
 ?
additional information HEPD oxidizes a relatively unactivated substrate that cannot easily facilitate O2 activation. 2-Hydroxyethylphosphonate does not contain a thiol group that upon binding to the iron can activate it for catalysis, nor does it contain an 2-oxo acid functionality Streptomyces viridochromogenes DSM 40736 ?
-
 ?

Synonyms

Synonyms Comment Organism
HEPD
-
 Streptomyces viridochromogenes
phpD
-
 Streptomyces viridochromogenes

General Information

General Information Comment Organism
evolution one group of mononuclear non-heme iron-dependent enzymes includes 2-hydroxyethylphosphonate dioxygenase (HEPD) and methylphosphonate synthase (MPnS, EC 1.13.11.73) that both carry out the oxidative cleavage of the carbon-carbon bond of 2-hydroxyethylphosphonate but generate different products. Common properties include the initial substrate oxidation by a ferric-superoxo-intermediate and a second oxidation by a ferryl species. Sequence homology between HEPD and MPnS combined with identical requirements for catalysis suggests a consensus mechanism in which product identity is determined by branching at an intermediate in the catalytic cycle Streptomyces viridochromogenes
additional information the active site metal is coordinated by 2-His-1-Glu on one face of a pseudooctrahedron Streptomyces viridochromogenes