MarketPeptidylglycine alpha-amidating monooxygenase
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Peptidylglycine alpha-amidating monooxygenase

Peptidyl-glycine alpha-amidating monooxygenase, or PAM, is an enzyme that catalyzes the conversion of an n+1 residue long peptide with a C-terminal glycine into an n-residue peptide with a terminal amide group. In the process, one molecule of O2 is consumed and the glycine residue is removed from the peptide and converted to glyoxylic acid.

Function
This gene encodes a multifunctional protein. It has two enzymatically active domains with catalytic activities - peptidylglycine alpha-hydroxylating monooxygenase (PHM) and peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL). These catalytic domains work sequentially to catalyze neuroendocrine peptides to active alpha-amidated products. The reaction pathway catalyzed by PAM is accessed via quantum tunneling and substrate preorganization. Multiple alternatively spliced transcript variants encoding different isoforms have been described for this gene, but some of their full-length sequences are not yet known. The PAL subunit then completes the conversion, by catalyzing elimination from the hydroxylated glycine: :peptide-C(O)NHCH(OH)CO2− → peptide-C(O)NH2 + CH(O)CO2− The eliminated coproduct is glyoxylate, written above as CH(O)CO2−. In insects Insect PαAMs are responsive to O concentrations and depends upon Cu. Simpson et al 2015 finds insect PαAMs to respond to hypoxia by regulating the activity of several peptide hormones. They find PαAM to probably be an important part of neuroendocrine responses to hypoxia. == References ==
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