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Literature summary for 1.14.17.3 extracted from

  • Barratt, B.J.; Easton, C.J.; Henry, D.J.; Li, I.H.; Radom, L.; Simpson, J.S.
    Inhibition of peptidylglycine alpha-amidating monooxygenase by exploitation of factors affecting the stability and ease of formation of glycyl radicals (2004), J. Am. Chem. Soc., 126, 13306-13311.
    View publication on PubMed
Search for more literature for 1.14.17.3

Inhibitors

Inhibitors Comment Organism Structure
gamma-keto acid
-
 Rattus norvegicus
glycolate
-
 Rattus norvegicus
additional information inhibition of peptidylglycine alpha-amidating monooxygenase by exploitation of factors affecting the stability and ease of formation of glycyl radicals, diverse glycine derivatives or substitutes, overview Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3
-
 N-benzoylglycine
-
 Rattus norvegicus
4.1
-
 N-trifluoroacetylglycine
-
 Rattus norvegicus
9.3
-
 N-acetylglycine
-
 Rattus norvegicus

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ required for peptidylglycine alpha-hydroxylating monooxygenase Rattus norvegicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Rattus norvegicus enzyme catalyzes the biosynthesis of peptide hormones through radical cleavage of the C-terminal glycine residues of the corresponding prohormones ?
-
 ?
peptidylglycine + ascorbate + O2 Rattus norvegicus peptidylglycine alpha-hydroxylating monooxygenase reaction peptidyl(2-hydroxylglycine) + 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
-
 bifunctional enzyme showing peptidylglycine alpha-hydroxylating monooxygenase, PHM, EC 1.14.17.3, and peptidylamidoglycolate lyase, PAL, EC 4.3.2.5, activities
-

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, PHM, EC 1.14.17.3, and peptidylamidoglycolate lyase, PAL, EC 4.3.2.5, activities Rattus norvegicus
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information enzyme catalyzes the biosynthesis of peptide hormones through radical cleavage of the C-terminal glycine residues of the corresponding prohormones Rattus norvegicus ?
-
 ?
additional information substrate specificity, effects of substitutions on the glycine substrate, overview Rattus norvegicus ?
-
 ?
N-acetylglycine + ascorbate + O2
-
 Rattus norvegicus N-acetyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
 ?
N-benzoylglycine + ascorbate + O2
-
 Rattus norvegicus N-benzoyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
 ?
N-trifluoroacetylglycine + ascorbate + O2
-
 Rattus norvegicus N-trifluoroacetyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
 ?
peptidylglycine + ascorbate + O2 peptidylglycine alpha-hydroxylating monooxygenase reaction, diverse glycine derivatives or substitutes 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 ?
peptidylglycine + ascorbate + O2 peptidylglycine alpha-hydroxylating monooxygenase reaction Rattus norvegicus peptidyl(2-hydroxylglycine) + dehydroascorbate + H2O the carbinol is the substrate for the peptidylamidoglycolate lyase reaction, EC 4.3.2.5, forming glyoxylate and amidated peptide ?

Cofactor

Cofactor Comment Organism Structure
ascorbate
-
 Rattus norvegicus