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Literature summary for 1.13.11.78 extracted from

  • Zhao, C.; Chen, H.
    Mechanism of organophosphonate catabolism by diiron oxygenase PhnZ a third iron-mediated O-O activation scenario in nature (2017), ACS Catal., 7, 3521-3531 .
No PubMed abstract available
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Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ required and involvedin catalysis. PhnZ is a nonheme diiron oxygenase uncultured bacterium HF130_AEPn_1

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(2-amino-1-hydroxyethyl)phosphonate + O2 uncultured bacterium HF130_AEPn_1
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 glycine + phosphate
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 ?

Organism

Organism UniProt Comment Textmining
uncultured bacterium HF130_AEPn_1 D0E8I5
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-

Reaction

Reaction Comment Organism Reaction ID
(2-amino-1-hydroxyethyl)phosphonate + O2 = glycine + phosphate PhnZ oxidatively cleaves the highly stable C-P bond in Pn to produce phosphate. Quantum mechanics/molecular mechanics (QM/MM) calculations reveal that the mechanism of PhnZ consists of four consecutive steps: (1) rate-limiting alpha-H abstraction of Pn by FeIII-superoxo, (2) formation of FeIIIOOCalpha peroxide, (3) concerted O insertion into Calpha-P bond of organophosphonate initiated by inverse heterolytic O-O cleavage, and (4) phosphonate hydrolysis to glycine and phosphate. Inverse heterolytic O-O cleavage of FeIIIOOCalpha intermediate renders the distal O atom more oxidative to oxygenate organophosphonate than the homolytic O-O cleavage. The unusual inverse heterolytic O-O cleavage mode constitutes a third iron-mediated O-O activation scenario in nature, which is expected to have its broad occurrence in oxidative transformation involving heteroatoms of sulfur and phosphorus, possible enzymatic O-O cleavage mechanisms from FeIII/IIOOR(H) intermediates, and electronic structure of resting state and superoxo intermediates, overview uncultured bacterium HF130_AEPn_1
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(2-amino-1-hydroxyethyl)phosphonate + O2
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 uncultured bacterium HF130_AEPn_1 glycine + phosphate
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 ?
(2-amino-1-hydroxyethyl)phosphonate + O2 substrate binding structure uncultured bacterium HF130_AEPn_1 glycine + phosphate
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 ?

Synonyms

Synonyms Comment Organism
ALOHA_HF130_AEPn_1_06c
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 uncultured bacterium HF130_AEPn_1
diiron oxygenase
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 uncultured bacterium HF130_AEPn_1
phnZ
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 uncultured bacterium HF130_AEPn_1

General Information

General Information Comment Organism
evolution the enzyme is a member of the HD-domain protein superfamily uncultured bacterium HF130_AEPn_1
metabolism combined with PhnY, which is a nonheme mononuclear 2-oxoglutarate-dependent dioxygenase to effect typical hydroxylation transformation of 2-amino-ethylphosphonic acid (2-AEP) to (R)-OH-AEP, the PhnY-PhnZ relay pathway affords aquatic and marine bacteria in Pi limited environments to utilize 2-AEP, the most abundant environmental 2-AEP, as the source of phosphate uncultured bacterium HF130_AEPn_1
physiological function diiron oxygenase PhnZ catalyzes the catabolism of organophosphonate (R)-2-amino-1-hydroxyethylphosphonic to glycine and inorganic phosphate (Pi). In this organophosphonate catabolism way, PhnZ oxidatively cleaves the highly stable C-P bond in Pn to produce phosphate. The reaction affords aquatic and marine bacteria in phosphate-limited environments to utilize the most abundant environmental organophosphonate 2-amino-ethylphosphonic acid as source of phosphate uncultured bacterium HF130_AEPn_1