Peptidylglycine alpha amidating enzyme sex dating in baxter tennessee
PHM and DBH share a few regions of sequence similarity, some of which contain clusters of conserved histidine residues that may be involved in copper binding [PMID: 11028916, PMID: 16301310].
Interestingly, in Drosophila, the PHM and PAL enzyme are not fused.
The Drosophila genome predicts expression of one monofunctional PHM gene and two monofunctional PAL genes [PMID: 15198673].
Drosophila PHM encodes an active enzyme that is required for peptide amidation in vivo [PMID: 10993678], while both PAL proteins display PAL enzymatic activity and are involved in neuroendocrine biosynthesis [PMID: 15198673].
The production of alpha-amidated peptides from their glycine-extended precursors is a two-step process involving the sequential action of two catalytic domains encoded by the bifunctional peptidylglycine alpha-amidating monooxygenase (PAM) precursor.