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Literature summary for 1.14.17.3 extracted from

  • Labrador, V.; Brun, C.; Konig, S.; Roatti, A.; Baertschi, A.J.
    Peptidyl-glycine alpha-amidating monooxygenase targeting and shaping of atrial secretory vesicles: inhibition by mutated N-terminal ProANP and PBA (2004), Circ. Res., 95, 98-109.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
single copy gene, alternative splicing generates several forms of enzyme mRNA, overview Rattus norvegicus

Inhibitors

Inhibitors Comment Organism Structure
4-Phenyl-3-butenoic acid binds to the lumenal side of the enzyme where the peptidylglycine alpha-hydroxylating PHM activity is localized Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane transmembrane protein with lumenal and cytoplasmic parts, overview, abundant in atrial secretory vesicles Rattus norvegicus 16020
-
vesicle from atrial myocytes, enzyme is recruited by aggregates of pro-atrial natriuretic peptide proANP, N-terminally deleted proANP is inhibited in recruiting the enzyme Rattus norvegicus 31982
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
90000
-
x * 125000, PAM-1, SDS-PAGE, x * 110000, PAM-2, SDS-PAGE, x * 90000, PAM-3, SDS-PAGE Rattus norvegicus
110000
-
x * 125000, PAM-1, SDS-PAGE, x * 110000, PAM-2, SDS-PAGE, x * 90000, PAM-3, SDS-PAGE Rattus norvegicus
125000
-
x * 125000, PAM-1, SDS-PAGE, x * 110000, PAM-2, SDS-PAGE, x * 90000, PAM-3, SDS-PAGE Rattus norvegicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Rattus norvegicus enzyme might be involved in secretory vesicle budding and fusion in the cardiac ANP-secretory pathway ?
-
?
peptidylglycine + ascorbate + O2 Rattus norvegicus peptidylglycine alpha-hydroxylating monooxygenase reaction peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O the carbinol is the substrate for the peptidylamidoglycolate lyase reaction, EC 4.3.2.5, forming glyoxylate and amidated peptide ?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
Sprague-Dawley, at least 3 different splicing variants PAM-1, PAM-2, and PAM-3
-

Reaction

Reaction Comment Organism Reaction ID
[peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O bifunctional enzyme showing peptidylglycine alpha-hydroxylating monooxygenase, EC 1.14.17.3, and peptidylamidoglycolate lyase, PAL, EC 4.3.2.5, activities, the enzyme possesses 2 catalytic domains Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
atrial appendage from neonatal rats Rattus norvegicus
-
atrium
-
Rattus norvegicus
-
heart
-
Rattus norvegicus
-
myocyte atrial myocyte Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information enzyme might be involved in secretory vesicle budding and fusion in the cardiac ANP-secretory pathway Rattus norvegicus ?
-
?
peptidylglycine + ascorbate + O2 peptidylglycine alpha-hydroxylating monooxygenase reaction Rattus norvegicus peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O the carbinol is the substrate for the peptidylamidoglycolate lyase reaction, EC 4.3.2.5, forming glyoxylate and amidated peptide ?

Subunits

Subunits Comment Organism
? x * 125000, PAM-1, SDS-PAGE, x * 110000, PAM-2, SDS-PAGE, x * 90000, PAM-3, SDS-PAGE Rattus norvegicus
More enzyme PAM-1, the longest transcript, is composed of, at the lumenal side, the peptidylglycine alpha-hydroxylating monooxygenase PHM catalytic domain, a noncatalytic domain from exon A, the peptidyl-alpha-hydroxyglacine alpha-amidating lyase PAL catalytic domain, a transmembrane domain, and a C-terminal cytoplasmic domain, deletion of exon A yields PAM-2, further deletion of the transmembrane domain yields soluble PAM-3 within the vesicle lumen Rattus norvegicus

Synonyms

Synonyms Comment Organism
PAM
-
Rattus norvegicus
peptidyl-glycine alpha-amidating monooxygenase
-
Rattus norvegicus

Cofactor

Cofactor Comment Organism Structure
ascorbate
-
Rattus norvegicus