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Peptidyl glycine hydroxylase

Ascorbic acid has specific and weU-deflned roles in two classes of enzymes the copper-containing hydroxylases (such as dopamine /3-hydroxylase and peptidyl glycine hydroxylase) and the 2-oxoglutarate-linked iron-containing hydroxylases, of which the best studied are the proline and lysine hydroxylases involved in maturation of connective tissue (and other) proteins. [Pg.364]

Figure 13.5. Reactions of peptidyl glycine hydroxylase (EC 1.14.17.3) and peptidyl hydroxygiycine a-amidating lyase (EC 4.3.2.5). Figure 13.5. Reactions of peptidyl glycine hydroxylase (EC 1.14.17.3) and peptidyl hydroxygiycine a-amidating lyase (EC 4.3.2.5).
Ascorbic acid functions as a relatively nonspecific, radical-trapping antioxidant and also reduces the tocopheroxyl radical formed by oxidation of vitamin E. It has a specific metabolic function as the redox coenzyme for dopamine /3-hydroxylase and peptidyl glycine hydroxylase, and it is required to maintain the iron of 2-oxoglutarate-dependent hydroxylases in the reduced state. [Pg.48]

PEPTIDYL GLYCINE a-AMIDATING MONOOXYGENASE Peptidylglycine 2-hydroxylase,... [Pg.769]

The second strategy is utilised by two other enzymes with a type 2 Cu centre, which in addition require ascorbate. Peptidyl-glycine a-hydroxylating monooxygenase (PMH), which converts C-terminal glycine-extended peptides to their a-hydroxylated products (Equation 1), and dopamine p-hydroxylase (OPH), which converts dopamine to noradrenahne (Equation 2) ... [Pg.283]

See other pages where Peptidyl glycine hydroxylase is mentioned: [Pg.366]    [Pg.366]    [Pg.506]    [Pg.366]    [Pg.366]    [Pg.509]    [Pg.366]    [Pg.366]    [Pg.509]    [Pg.366]    [Pg.366]    [Pg.506]    [Pg.366]    [Pg.366]    [Pg.509]    [Pg.366]    [Pg.366]    [Pg.509]    [Pg.131]    [Pg.282]    [Pg.158]    [Pg.347]    [Pg.49]    [Pg.30]    [Pg.5496]    [Pg.5792]    [Pg.5495]    [Pg.5791]   
See also in sourсe #XX -- [ Pg.49 ]



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