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In enzymology, a 4-hydroxybenzoate 3-monooxygenase () is an enzyme that catalyzes the chemical reaction :4-hydroxybenzoate + NADPH + H+ + O2 protocatechuate + NADP+ + H2O The 4 substrates of this enzyme are 4-hydroxybenzoate, NADPH, H+, and O2, whereas its 3 products are protocatechuate, NADP+, and H2O. This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is 4-hydroxybenzoate,NADPH:oxygen oxidoreductase (3-hydroxylating). Other names in common use include p-hydroxybenzoate hydrolyase, p-hydroxybenzoate hydroxylase, 4-hydroxybenzoate 3-hydroxylase, 4-hydroxybenzoate monooxygenase, 4-hydroxybenzoic hydroxylase, p-hydroxybenzoate-3-hydroxylase, p-hydroxybenzoic acid hydrolase, p-hydroxybenzoic acid hydroxylase, and p-hydroxybenzoic hydroxylase. This enzyme participates in benzoate degradation via hydroxylation and 2,4-dichlorobenzoate degradation. It employs one cofactor, FAD. ==Structural studies== As of late 2007, 31 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , and . 抄文引用元・出典: フリー百科事典『 ウィキペディア(Wikipedia)』 ■ウィキペディアで「4-hydroxybenzoate 3-monooxygenase」の詳細全文を読む スポンサード リンク
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