Acireductone synthase

Definition:

EC Tree > 3 Hydrolases > 3.1 Acting on ester bonds > 3.1.3 Phosphoric-monoester hydrolases > 3.1.3.77 acireductone synthase
Acireductone synthase is a bifunctional methionine-salvage enzyme that first enolises 5-(methylsulfanyl)-2,3-dioxopentyl phosphate into the intermediate 2-hydroxy-5-(methylsulfanyl)-3-oxopent-1-enyl phosphate, and then dephosphorylates it to yield the acireductone 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one, releasing inorganic phosphate. The acireductone sits at a branch point: Ni2+-requiring acireductone dioxygenase (EC 1.13.11.53) converts it into formate, CO and 3-(methylsulfanyl)propanoate, whereas Fe(II)-requiring acireductone dioxygenase (EC 1.13.11.54) or an aerobic spontaneous reaction yields formate and 4-(methylsulfanyl)-2-oxobutanoate, the precursor of methionine. It is distributed across Eukaryota and Bacteria and combines an enolase-like domain with a HAD-like phosphatase domain.

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