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Literature summary 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

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.3.2.5 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 ?
-
 ?
4.3.2.5 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 ?
-
 ?
4.3.2.5 peptidylamidoglycolate Mus musculus
-
 peptidyl amide + glyoxylate
-
 ?
4.3.2.5 peptidylamidoglycolate Mus musculus C57/BL6J
-
 peptidyl amide + glyoxylate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.3.2.5 Mus musculus
-
-
-
4.3.2.5 Mus musculus C57/BL6J
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
4.3.2.5 pituitary gland
-
 Mus musculus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.3.2.5 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 ?
-
 ?
4.3.2.5 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 ?
-
 ?
4.3.2.5 peptidylamidoglycolate
-
 Mus musculus peptidyl amide + glyoxylate
-
 ?
4.3.2.5 peptidylamidoglycolate
-
 Mus musculus C57/BL6J peptidyl amide + glyoxylate
-
 ?

Synonyms

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

General Information

EC Number General Information Comment Organism
4.3.2.5 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