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Literature summary for 4.3.2.5 extracted from

  • Yin, P.; Bousquet-Moore, D.; Annangudi, S.P.; Southey, B.R.; Mains, R.E.; Eipper, B.A.; Sweedler, J.V.
    Probing the production of amidated peptides following genetic and dietary copper manipulations (2011), PLoS ONE, 6, e28679.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.3.2.5

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Mus musculus in the amidation reaction, the reactant (glycine-extended peptide) is converted into a reaction intermediate (hydroxyglycine-extended peptide) by the copper-dependent peptidylglycine-alpha-hydroxylating monooxygenase (PHM) domain of PAM. The hydroxyglycine-extended peptide is then converted into amidated product by the peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) domain of PAM ?
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 ?
additional information Mus musculus C57/BL6J in the amidation reaction, the reactant (glycine-extended peptide) is converted into a reaction intermediate (hydroxyglycine-extended peptide) by the copper-dependent peptidylglycine-alpha-hydroxylating monooxygenase (PHM) domain of PAM. The hydroxyglycine-extended peptide is then converted into amidated product by the peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) domain of PAM ?
-
 ?
peptidylamidoglycolate Mus musculus
-
 peptidyl amide + glyoxylate
-
 ?
peptidylamidoglycolate Mus musculus C57/BL6J
-
 peptidyl amide + glyoxylate
-
 ?

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-
Mus musculus C57/BL6J
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
pituitary gland
-
 Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information in the amidation reaction, the reactant (glycine-extended peptide) is converted into a reaction intermediate (hydroxyglycine-extended peptide) by the copper-dependent peptidylglycine-alpha-hydroxylating monooxygenase (PHM) domain of PAM. The hydroxyglycine-extended peptide is then converted into amidated product by the peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) domain of PAM Mus musculus ?
-
 ?
additional information in the amidation reaction, the reactant (glycine-extended peptide) is converted into a reaction intermediate (hydroxyglycine-extended peptide) by the copper-dependent peptidylglycine-alpha-hydroxylating monooxygenase (PHM) domain of PAM. The hydroxyglycine-extended peptide is then converted into amidated product by the peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) domain of PAM Mus musculus C57/BL6J ?
-
 ?
peptidylamidoglycolate
-
 Mus musculus peptidyl amide + glyoxylate
-
 ?
peptidylamidoglycolate
-
 Mus musculus C57/BL6J peptidyl amide + glyoxylate
-
 ?

Synonyms

Synonyms Comment Organism
PAL
-
 Mus musculus
peptidyl-alpha-hydroxyglycine alpha-amidating lyase
-
 Mus musculus

General Information

General Information Comment Organism
additional information the the peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) is located on a domain of peptidylglycine alpha-amidating monooxygenase (PAM). The monooxygenase reaction is a slower step in peptide amidation, so that in peptidylglycine alpha-amidating monooxygenase (PAM) deficient mice, peptidyl-alpha-hydroxyglycine alpha-amidating lyase becomes the limiting factor of conversion of amidated peptides, overview. Peptidylglycine-alpha-hydroxylating monooxygenase, PHM, and peptidyl-alpha-hydroxyglycine alpha-amidating lyase, PAL, are stitched together in most vertebrates, kinetic studies with purified PHM and PAL revealed a higher affinity of PHM for its peptide substrate and a higher turnover number for PAL Mus musculus