Crystallization (Comment) | Organism |
---|---|
molecular dynamics simulations based onthe crystal structure 1SDW, overview | Rattus norvegicus |
Protein Variants | Comment | Organism |
---|---|---|
Q170A | site-directed mutagenesis, mutant enzyme activity as a function of the number of hydrogen bonds established in the bridge between the two copper ions compared to the wild-type enzyme | Rattus norvegicus |
Q170E | site-directed mutagenesis, mutant enzyme activity as a function of the number of hydrogen bonds established in the bridge between the two copper ions compared to the wild-type enzyme | Rattus norvegicus |
Q170L | site-directed mutagenesis, mutant enzyme activity as a function of the number of hydrogen bonds established in the bridge between the two copper ions compared to the wild-type enzyme | Rattus norvegicus |
Q170N | site-directed mutagenesis, mutant enzyme activity as a function of the number of hydrogen bonds established in the bridge between the two copper ions compared to the wild-type enzyme | Rattus norvegicus |
Y79W | site-directed mutagenesis, mutant enzyme activity as a function of the number of hydrogen bonds established in the bridge between the two copper ions compared to the wild-type enzyme | Rattus norvegicus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Cu2+ | a noncoupled dicopper enzyme | Rattus norvegicus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
peptidyl-glycine + ascorbate + O2 | Rattus norvegicus | - |
peptidyl-(2-hydroxylglycine) + dehydroascorbate + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rattus norvegicus | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | long distance electron-transfer mechanism between the two distant copper cations, a perfect fitting for a water bridge, molecular dynamics simulations using wild-type and mutant enzymes, overview | Rattus norvegicus | ? | - |
? | |
peptidyl-glycine + ascorbate + O2 | - |
Rattus norvegicus | peptidyl-(2-hydroxylglycine) + dehydroascorbate + H2O | - |
? | |
peptidyl-glycine + ascorbate + O2 | PHM catalyzes the stereospecific hydroxylation of the glycine alpha-carbon of all peptidylglycine substrates | Rattus norvegicus | peptidyl-(2-hydroxylglycine) + dehydroascorbate + H2O | - |
? |
Synonyms | Comment | Organism |
---|---|---|
peptidylglycine alpha-hydroxylating monooxygenase | - |
Rattus norvegicus |
PHM | - |
Rattus norvegicus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
5.5 | 7 | assay at | Rattus norvegicus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ascorbate | - |
Rattus norvegicus |