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Peptidyl glycine a-amidating monooxygenase

MONOPHENOL MONOOXYGENASE NITRIC OXIDE SYNTHASE PEPTIDYL GLYCINE a-AMIDATING MONOOXYGENASE... [Pg.768]

PEPTIDYL GLYCINE a-AMIDATING MONOOXYGENASE Peptidylprolyl ds-trans isomerase,... [Pg.769]

An unusual method for chain termination is utilized in the biosynthesis of myxothiazol and melithiazol. The domains in the terminal modules of these synthetases are arranged in the following order C-A-MOx-A-PCP-TE (MOx = monooxygenase domain). In the termination modules of these synthetases, the MOx domain likely catalyzes hydroxylation of the ct-carhon of the C-terminal glycine residue of the requisite peptidyl-5-PCP. The resulting intermediate then undergoes spontaneous conversion into PCP-bound glyoxylic acid and a terminal amide. This sequence yields the final product in the case of myxothiazol, whereas the terminal amide is transformed to a methyl ester to complete melithiazol biosynthesis. [Pg.635]

See other pages where Peptidyl glycine a-amidating monooxygenase is mentioned: [Pg.541]    [Pg.769]    [Pg.769]    [Pg.131]    [Pg.242]    [Pg.589]    [Pg.158]    [Pg.347]    [Pg.236]    [Pg.541]    [Pg.769]    [Pg.769]    [Pg.131]    [Pg.242]    [Pg.589]    [Pg.158]    [Pg.347]    [Pg.236]    [Pg.244]    [Pg.508]    [Pg.5792]    [Pg.5791]    [Pg.379]    [Pg.231]   
See also in sourсe #XX -- [ Pg.87 ]



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