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Literature summary for 3.5.2.15 extracted from

  • Peat, T.S.; Balotra, S.; Wilding, M.; French, N.G.; Briggs, L.J.; Panjikar, S., Cowieson, N.; Newman, J.; Scott, C.
    Cyanuric acid hydrolase: evolutionary innovation by structural concatenation (2013), Mol. Microbiol., 88, 1149-1163.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
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Pseudomonas sp.

Crystallization (Commentary)

Crystallization (Comment) Organism
Toblerone fold. Product of concatenation of three proteins of YjdF fold. PDB IDs 4BVT, 4BVS, 4BVR, 4BVQ, native enzyme and in complex with melamine, barbituric acid, and cyanuric acid and Xe-derivative, to 1.9, 2.6, 3.1, 2.6 and 2.55 A resolution, respectively. The AtzD monomer, active site and substrate all possess threefold rotational symmetry, to the extent that the active site possesses three potential Ser–Lys catalytic dyads. A single catalytic dyad, Ser85–Lys42, is hypothesized, based on biochemical evidence and crystallographic data Pseudomonas sp.

Organism

Organism UniProt Comment Textmining
Pseudomonas sp. P58329
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information hypothetical reaction mechanism consistent with a Ser85 nucleophile. Lys42 is a general base, activating Ser85 and promoting formation of a tetrahedral intermediate between Ser85 and the closest substrate carbonyl carbon, this then resolves into the acyl:enzyme intermediate following ring opening. Thereafter, a solvent water molecule is required to hydrolyse the acyl intermediate and regenerate the serine, liberating carboxybiuret Pseudomonas sp. ?
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