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Literature summary for 3.11.1.2 extracted from

  • Agarwal, V.; Borisova, S.A.; Metcalf, W.W.; van der Donk, W.A.; Nair, S.K.
    Structural and mechanistic insights into C-P bond hydrolysis by phosphonoacetate hydrolase (2011), Chem. Biol., 18, 1230-1240.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.11.1.2

Crystallization (Commentary)

Crystallization (Comment) Organism
X-ray diffraction structure determination and analysis at 1.35 A resolution, cocrystal structures with phosphonoacetate substrate, acetate, phosphonoformate inhibitor, and a covalently bound transition state mimic Sinorhizobium meliloti

Inhibitors

Inhibitors Comment Organism Structure
Phosphonoformate
-
 Sinorhizobium meliloti

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Phosphonoacetate + H2O Sinorhizobium meliloti
-
 acetate + phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Sinorhizobium meliloti Q92UV8 gene phnA
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Phosphonoacetate + H2O
-
 Sinorhizobium meliloti acetate + phosphate
-
 ?

Synonyms

Synonyms Comment Organism
PhnA
-
 Sinorhizobium meliloti

General Information

General Information Comment Organism
metabolism 2-aminoethylphosphonate is catabolized to phosphonoacetate, which is converted to acetate and inorganic phosphate by phosphonoacetate hydrolase, PhnA Sinorhizobium meliloti
additional information C-P bond hydrolysis by phosphonoacetate hydrolase, structure and mechanism, overview. Structure analysis of bound substrate, product, inhibitor, and a covalently bound transition state mimic provide insight into active site features that may facilitate cleavage of the C-P bond Sinorhizobium meliloti