EC Number |
General Information |
Reference |
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1.13.11.78 | 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 |
743680 |
1.13.11.78 | evolution |
the enzyme is a member of the HD-domain protein superfamily |
743907 |
1.13.11.78 | 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 |
743907 |
1.13.11.78 | more |
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 |
743680 |
1.13.11.78 | 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 |
743907 |
1.13.11.78 | 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 |
743680 |