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1 ly of aromatic hydroxylases characterized by p-hydroxybenzoate hydroxylase.
2 overall fold of 3HB6H is similar to that of p-hydroxybenzoate hydroxylase and other flavoprotein aro
3 some flavin-dependent hydroxylases (notably, p-hydroxybenzoate hydroxylase), binding of the hydroxyla
6 ubstrate analog, p-aminobenzoate, binding to p-hydroxybenzoate hydroxylase have been elicited by Rama
10 of several complexes involving FAD bound to p-hydroxybenzoate hydroxylase (PHBH) have revealed that
16 ructure can be assigned to the well-studied, p-hydroxybenzoate hydroxylase (PHBH) SCOP superfamily of
17 rall architecture is most similar to that of p-hydroxybenzoate hydroxylase (PHBH), although there are
18 es have revealed two flavin conformations in p-hydroxybenzoate hydroxylase (PHBH), the in-position an
23 y step in the paradigm aromatic hydroxylase, p-hydroxybenzoate hydroxylase (PHBH): the oxidation of p
25 g that the control of the flavin position in p-hydroxybenzoate hydroxylase represents a compromise be
27 le of catalysis in RebC may resemble that of p-hydroxybenzoate hydroxylase, with substrate binding pr
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