Function and Structure of Peptide α-Amidating Monooxygenase
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    Abstract:

    Carboxy-terminal amidation is an essential posttranslational modification for numerous neuronal and endocrine peptides.It is catalyzed by peptide α-amidating monooxygenase (PAM),in a two-step reaction. Peptidylglycine α-hydroxylating monooxygenase(PHM) and peptidyl-hydroxyglycine -α-amidating lyase(PAL) act in one of the two step.PHM catalytic core is composed of two nine-stranded β-sandwich domains similar in three-dimessional structure.Each domain contains an activity center with a copper coordinated by three conserved His or two His and a Met residues.In the reaction cycle of producing peptidyl α-hydroxyglycine,the two coppers are reduced independently by ascorbate,and they transfer one electron each to molecular oxygen.

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LIU Shen-Ji, CHEN Song-Sen. Function and Structure of Peptide α-Amidating Monooxygenase[J]. Progress in Biochemistry and Biophysics,1999,26(3):195-197

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History
  • Received:April 20,1998
  • Revised:December 31,1998
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