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Literature summary for 1.14.17.3 extracted from
- Long distance electron-transfer mechanism in peptidylglycine alpha-hydroxylating monooxygenase: a perfect fitting for a water bridge (2007), J. Am. Chem. Soc., 129, 11700-11707.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| molecular dynamics simulations based onthe crystal structure 1SDW, overview | Rattus norvegicus |
Protein Variants
| 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
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Cu2+ | a noncoupled dicopper enzyme | Rattus norvegicus |  |
Natural Substrates/ Products (Substrates)
| 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
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rattus norvegicus | - |
- |
- |
Substrates and Products (Substrate)
| 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
| Synonyms | Comment | Organism |
|---|---|---|
| peptidylglycine alpha-hydroxylating monooxygenase | - |
Rattus norvegicus |
| PHM | - |
Rattus norvegicus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5.5 | 7 | assay at | Rattus norvegicus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ascorbate | - |
Rattus norvegicus | |
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Release 2023.1 (January 2023)
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