Peptidylglycine alpha amidating ryan sheckler dating chanel west coast

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Each domain is about 150 residues long and binds one catalytic Cu ().

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The catalytic core of PHM consists of two β-clamshell or sandwich domains.

Each approximately 150-amino acid domain contains a single copper binding site. The two domains are held together by a single hydrophilic linker strand, whereas the interiors of the domains are very hydrophobic.

The X-ray structure places the two copper ions 11 Å apart and separated by a solvent-filled cleft; the Gly-extended peptide substrate binds closer to Cu.

Dopamine β-monooxygenase shares many conserved disulfide bonds and contains histidine and methionine residues that may bind to copper in a similar manner.

Elimination of the exon encoding the transmembrane domain yields a soluble, secreted enzyme.

Peptidylglycine alpha amidating

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