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Literature summary for 1.14.17.3 extracted from

  • Suzuki, K.; Shimoi, H.; Iwasaki, Y.; Kawahara, T.; Matsuura, Y.; Nishikawa, Y.
    Elucidation of amidating reaction mechanism by frog amidating enzyme, peptidylglycine alpha-hydroxylating monooxygenase, expressed in insect cell culture (1990), EMBO J., 9, 4259-4265.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Spodoptera fugiperda cells via baculovirus vector, amino acid sequence analysis Xenopus laevis

Inhibitors

Inhibitors Comment Organism Structure
EDTA
-
Xenopus laevis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0032
-
N-dansyl-Tyr-Phe-Gly + 2 mM L-ascorbate Xenopus laevis
0.28
-
L-ascorbate + 0.02 mM N-dansyl-Tyr-Phe-Gly Xenopus laevis

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ a copper protein Xenopus laevis
Cu2+ Cu2+ is absolutely required for optimal activity Xenopus laevis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
39000
-
SDS-PAGE, gel filtration Xenopus laevis
39000
-
native wild-type enzyme Xenopus laevis
43000
-
recombinant wild-type enzyme, SDS-PAGE, gel filtration Xenopus laevis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
peptidylglycine + ascorbate + O2 Xenopus laevis
-
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
?

Organism

Organism UniProt Comment Textmining
Xenopus laevis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
native wild-type and recombinant from Spodoptera frugiperda cell expression system Xenopus laevis

Reaction

Reaction Comment Organism Reaction ID
[peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O mechanism Xenopus laevis

Source Tissue

Source Tissue Comment Organism Textmining
skin
-
Xenopus laevis
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
16
-
purified recombinant enzyme Xenopus laevis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Ala-Ile-Gly-Val-Gly-Ala-Pro-Gly + ascorbate + O2
-
Xenopus laevis Ala-Ile-Gly-Val-Gly-Ala-Pro-2-hydroxyglycine + dehydroascorbate + H2O
-
?
dansyl-D-Tyr-Val-Gly + ascorbate + O2
-
Xenopus laevis dansyl-D-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
-
?
additional information EC 1.14.17.3 is often called peptidylglycine alpha-amidating monooxygenase (PAM) and the alpha-amidated product is mentioned as the product of the reaction, but the alpha-amidation of glycine-extended peptides is a two-step process catalyzed by 2 enzymes: 1. EC 1.14.17.3: production of peptidyl(2-hydroxyglycine) by a copper, molecular oxygen and ascorbate-dependent peptidyl-glycine alpha-hydroxylating monooxygenase (PMH) and 2. conversion of the peptidyl-alpha-hydroxyglycine derivative into an alpha-amidated product at physiological pH by peptidyl-alpha-hydroxyglycine alpha-amidating lyase Xenopus laevis ?
-
?
N-dansyl-L-Tyr-L-Phe-Gly + ascorbate + O2
-
Xenopus laevis N-dansyl-L-Tyr-L-Phe-2-hydroxyglycine + dehydroascorbate + H2O
-
r
peptidylglycine + ascorbate + O2
-
Xenopus laevis peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
?
peptidylglycine + ascorbate + O2 COOH-terminal glycine Xenopus laevis peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
?

Synonyms

Synonyms Comment Organism
More EC 1.14.17.3 is often called peptidylglycine alpha-amidating monooxygenase (PAM) and the alpha-amidated product is mentioned as the product of the reaction, but the alpha-amidation of glycine-extended peptides is a two-step process catalyzed by 2 enzymes: 1. EC 1.14.17.3: production of peptidyl(2-hydroxyglycine) by a copper, molecular oxygen and ascorbate-dependent peptidyl-glycine alpha-hydroxylating monooxygenase (PHM), 2. conversion of the peptidyl-alpha-hydroxyglycine derivative into an alpha-amidated product at physiological pH by peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PHL) Xenopus laevis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Xenopus laevis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.4
-
assay at, recombinant enzyme Xenopus laevis
5.5 6
-
Xenopus laevis

Cofactor

Cofactor Comment Organism Structure
ascorbate dependent on Xenopus laevis