Literature summary 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.

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
3.11.1.2	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

EC Number	Inhibitors	Comment	Organism	Structure
3.11.1.2	Phosphonoformate	-	Sinorhizobium meliloti

Natural Substrates/ Products (Substrates)

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

Organism

EC Number	Organism	UniProt	Comment	Textmining
3.11.1.2	Sinorhizobium meliloti	Q92UV8	gene phnA	-

Substrates and Products (Substrate)

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

Synonyms

EC Number	Synonyms	Comment	Organism
3.11.1.2	PhnA	-	Sinorhizobium meliloti

General Information

EC Number	General Information	Comment	Organism
3.11.1.2	metabolism	2-aminoethylphosphonate is catabolized to phosphonoacetate, which is converted to acetate and inorganic phosphate by phosphonoacetate hydrolase, PhnA	Sinorhizobium meliloti
3.11.1.2	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

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Release 2023.1 (January 2023)