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Literature summary for 1.14.16.1 extracted from
- Regulation of phenylalanine hydroxylase: conformational changes upon phenylalanine binding detected by hydrogen/deuterium exchange and mass spectrometry (2010), Biochemistry, 49, 3327-3335.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| DELTA1-117 | mutant lacking the first 117 amino acids containing only the catalytic and tetramerization domains: the effects of phenylalanine on the hydrogen/deuterium exchange kinetics are limited to peptides surrounding the binding site for the amino acid substrate | Rattus norvegicus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rattus norvegicus | P04176 | - |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| L-phenylalanine + a 5,6,7,8-tetrahydropteridine + O2 = L-tyrosine + a 4a-hydroxy-5,6,7,8-tetrahydropteridine | hydrogen/deuterium exchange monitored by mass spectrometry is used to gain insight into local conformational changes accompanying activation of rat phenylalanine hydroxylase by phenylalanine. Peptides in the regulatory and catalytic domains that lie in the interface between these two domains show large increases in the extent of deuterium incorporation from solvent in the presence of phenylalanine | Rattus norvegicus |
aSynonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PheH | - |
Rattus norvegicus |
| phenylalanine hydroxylase | - |
Rattus norvegicus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Rattus norvegicus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
assay at | Rattus norvegicus |
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Release 2023.1 (January 2023)
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