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1.14.13.172: salicylate 5-hydroxylase

This is an abbreviated version!
For detailed information about salicylate 5-hydroxylase, go to the full flat file.

Word Map on EC 1.14.13.172

Reaction

salicylate
+
NADH
 +
H+
 +
O2
=
2,5-Dihydroxybenzoate
 +
NAD+
 +
H2O

Synonyms

nagG, NagGH, nagH, S5H, S5HR, SAL5H, SalABCD, SALD

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
                1.14.13.172 salicylate 5-hydroxylase

Crystallization

Crystallization on EC 1.14.13.172 - salicylate 5-hydroxylase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure of the oxygenase component NagGH. The large subunit NagG and small subunit NagH share the same fold as that for their counterparts of Rieske dioxygenases and assemble the same alpha3beta3 hexamer. A potential substrate-binding pocket is observed in the vicinity of the nonheme iron site. Its positively charged residue Arg323 is surrounded by hydrophobic residues. The shift of nonheme iron atom caused by residue Leu228 disrupts the usual substrate pocket observed in other Rieske oxygenases. Residue Asn218 is involved in substrate binding and oxidation, but residues Gln316 and Ser367 play a more important role in substrate oxidation than Asn218
O52378; O52381; O52379; O52380