Peptidylglycine alpha amidating ryan sheckler dating chanel west coast
Each domain is about 150 residues long and binds one catalytic Cu ().
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.