Peptidylglycine alpha amidating

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The first two domains are enzymes existing on the inside of the secretory granule, while the third domain is on the outside of the secretory granule.Some of our studies have focused on the enzymatic properties of the two enzymes, going as far as X-ray crystallography and other biophysical studies which are performed by our various collaborators using our proteins.The role of these non-catalytic domains seems to be in getting PAM to the right place in the cell so that it can do its job.In particular, the cytosolic domain is essential for targeting PAM to the secretory granules of pituitary endocrine cells and for guiding PAM protein that has reached the cell surface back into secretory granules following internalization.And the proopiomelanocortin neurons in the brain make other collections of peptides. Why do many sympathetic neurons make neuropeptide Y along with norepinephrine?

One key enzyme that has been a major focus of effort has been PAM [Fig.After mapping several key determinants in the rather short cytosolic domain of PAM, we identified proteins that interact with it.One of these proteins, PCIP-2 (Uhmk1) is a protein kinase that is highly selective for PAM.Hypothalamic peptides like oxytocin and vasopressin along with neuropeptides like substance P and gastrointestinal mediators like gastrin must be amidated in order to affect their target tissues.By purifying an enzyme capable of converting peptidylglycine precursors into amidated products, we were then able to clone a c DNA encoding this enzyme.

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