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Literature summary for 1.14.17.3 extracted from
- Functional expression and characterization of a Xenopus laevis peptidylglycine alpha-amidating monooxygenase, AE-II, in insect-cell culture (1993), Eur. J. Biochem., 213, 93-98.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Spodoptera fugiperda cells via baculovirus vector of membrane-associated, bifunctional enzyme form 2, AE-II, wild-type and truncated mutant, N-terminal amino acid sequence analysis | Xenopus laevis |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | construction of a truncated form of AE-II, lacking the transmembrane domain and leading to solubility of the fully active, truncated enzyme being secreted into the culture medium from Spodoptera frugiperda cells | Xenopus laevis |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| D-Tyr-Val-Gly | inhibition above 20 mM of hydroxylation | Xenopus laevis |  |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 3.5 | - |
N-dansyl-L-Tyr-L-Phe-Gly | recombinant mutant AE-II, form 2 | Xenopus laevis | |
| 3.5 | - |
N-dansyl-L-Tyr-L-Phe-Gly | reaction product of step 1, substrate of step 2 | Xenopus laevis | |
| 4.5 | - |
N-dansyl-L-Tyr-L-Phe-Gly | recombinant mutant AE-II, form 2 | Xenopus laevis |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | transmembranal protein | Xenopus laevis | 16020 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Cu2+ | - |
Xenopus laevis | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 74000 | - |
1 * 74000, recombinant mutant AE-II, form 2, SDS-PAGE | Xenopus laevis |
| 78000 | - |
recombinant mutant AE-II, form 2, 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 | - |
3 genetic forms, 2 protein forms of amidating enzyme: protein form 1, gene AE-I, has only peptidylglycine alpha-hydroxylating activity, protein form 2, genes AE-III and AE-II, show peptidylglycine alpha-hydroxylating activity and peptidylhydroxylglycine N-C lyase activity | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| truncated mutant form 2 from gene AE-II, recombinant from Spodoptera frugiperda cell expression system | Xenopus laevis |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| skin | soluble enzyme with peptidylglycine alpha-hydroxylating activity or peptidylhydroxylglycine N-C lyase activity | 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 | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer | 1 * 74000, recombinant mutant AE-II, form 2, SDS-PAGE | Xenopus laevis |
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 |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ascorbate | dependent on | Xenopus laevis | |
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