1.13.11.78: 2-amino-1-hydroxyethylphosphonate dioxygenase (glycine-forming)
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For detailed information about 2-amino-1-hydroxyethylphosphonate dioxygenase (glycine-forming), go to the full flat file.
Reaction
Synonyms
(R)-1-hydroxy-2-aminoethylphosphonate oxygenase, ALOHA_HF130_AEPn_1_06c, diiron oxygenase, phnZ
ECTree
1.13.11.78 2-amino-1-hydroxyethylphosphonate dioxygenase (glycine-forming)Advanced search results
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General Information on EC 1.13.11.78 - 2-amino-1-hydroxyethylphosphonate dioxygenase (glycine-forming)
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
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
physiological function
additional information
enzyme PhnZ has an active site containing two Fe ions coordinated by four histidines and two aspartates that is strikingly similar to the carbon-carbon bond cleaving enzyme, myo-inositol-oxygenase. The exception is residue Y24, which forms a transient ligand interaction at the dioxygen binding site of the second Fe2+. Structure comparisons and substrate binding structures, active site structure, detailed overview
evolution
enzyme PhnZ belongs to a large family of hydrolytic enzymes, the HD-phosphohydrolase superfamily, which comprises enzymes that use a strictly conserved His-Asp sequence motif to bind active site metal ions. Structural comparisons of PhnZ reveal an evolutionary connection between Fe(II)-dependent hydrolysis of phosphate esters and oxidative carbon-phosphorus or carbon-carbon bond cleavage, thus uniting the diverse chemistries that are found in the HD superfamily. PhnZ is a structural homologue of myo-inositol oxygenase and Fe(II)-dependent phosphohydrolases
evolution
the enzyme is a member of the HD-domain protein superfamily
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
physiological function
the enzymes PhnY and PhnZ comprise an oxidative catabolic pathway that enables marine bacteria to use 2-aminoethylphosphonic acid as a source of inorganic phosphate. PhnZ is notable for catalyzing the oxidative cleavage of a carbon-phosphorus bond using Fe(II) and dioxygen
