Coordination of peroxide to the CuM center of peptidylglycine α-hydroxylating monooxygenase (PHM): Structural and computational study

Many bioactive peptides, such as hormones and neuropeptides, require amidation at the C terminus for their full biological activity. Peptidylglycine α-hydroxylating monooxygenase (PHM) performs the first step of the amidation reaction - the hydroxylation of peptidylglycine substrates at the Cα posit...

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Detalles Bibliográficos
Autores principales:	Rudzka, K., Moreno, D.M., Eipper, B., Mains, R., Estrin, D.A., Amzel, L.M.
Formato:	JOUR
Materias:	Amidation of peptides Copper-containing proteins Peptidylglycine α-hydroxylating monooxygenase Peroxide copper H copper ion copper M cupric ion cuprous ion glycine hydrogen peroxide oxygen derivative oxygenase peptidylglycine alpha hydroxylating monooxygenase peroxide unclassified drug amidation animal cell article carboxy terminal sequence catalysis complex formation controlled study crystal structure energy enzyme active site enzyme binding enzyme metabolism female hamster hydroxylation isomer ligand binding molecular interaction molecular mechanics molecular model nonhuman priority journal quantum mechanics structure activity relation structure analysis X ray diffraction Animals Catalytic Domain CHO Cells Computer Simulation Coordination Complexes Copper Cricetinae Crystallography, X-Ray Hydrogen Bonding Hydrogen Peroxide Mixed Function Oxygenases Models, Molecular Multienzyme Complexes Quantum Theory Rats
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_09498257_v18_n2_p223_Rudzka
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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