Activating Compound | Comment | Organism | Structure |
---|---|---|---|
O2 | substrate binding triggers oxygen activation in peptidylglycine monooygenase | Rattus norvegicus |
Cloned (Comment) | Organism |
---|---|
recombinant expression of wild-type and mutant enzymes | Rattus norvegicus |
Protein Variants | Comment | Organism |
---|---|---|
H107A | site-directed mutagenesis, altered reaction with CO compared to wild-type | Rattus norvegicus |
H107A/H108A | site-directed mutagenesis, the double His mutant H107H108A binds copper only in the M-site and therefore contains about 1 equivalent copper per protein | Rattus norvegicus |
H108A | site-directed mutagenesis, altered reaction with CO compared to wild-type | Rattus norvegicus |
H242A | site-directed mutagenesis, the CuM site mutant which has an empty M site in the reduced state, does not react with CO in the presence or absence of peptide substrate | Rattus norvegicus |
M109I | site-directed mutagenesis, altered reaction with CO compared to wild-type | Rattus norvegicus |
M314H | site-directed mutagenesis, altered reaction with CO compared to wild-type | Rattus norvegicus |
M314I | site-directed mutagenesis, the CuM site mutant which has an empty M site in the reduced state, does not react with CO in the presence or absence of peptide substrate | Rattus norvegicus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Cu2+ | dependent on, two coopper ions, CuM is coordinated by His242, His244 and Met314, while CuH is bound to His107, His108, and His172. The catalytic reaction requires both copper ions to cycle between Cu(II) and Cu(I) oxidation states. Two conformations at CuM in which the second CO band depends on the mode of substrate binding and may thus report on a substrate-induced catalytically active configuration. Upon substrate addition, the lower (nyCO) band is amplified while the other decreases, but not at a 1:1 ratio, indicating an equilibrium which is shifted in the presence of substrate. Crystal structure of CuM and CuH sites, overview | Rattus norvegicus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
peptidylglycine + ascorbate + O2 | Rattus norvegicus | - |
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rattus norvegicus | P14925 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant wild-type and mutant enzymes | Rattus norvegicus |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
[peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O | equilibrium ordered mechanism in which substrate binds prior to oxygen | Rattus norvegicus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
peptidylglycine + ascorbate + O2 | - |
Rattus norvegicus | peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O | - |
? |
Synonyms | Comment | Organism |
---|---|---|
PHM | - |
Rattus norvegicus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ascorbate | - |
Rattus norvegicus |
General Information | Comment | Organism |
---|---|---|
additional information | substrate binding triggers oxygen activation in peptidylglycine monooygenase | Rattus norvegicus |