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Literature summary for 1.14.16.4 extracted from
- Enhancement of L-tryptophan 5-hydroxylation activity by structure-based modification of L-phenylalanine 4-hydroxylase from Chromobacterium violaceum (2009), J. Biosci. Bioeng., 108, 184-189.
Application
| Application | Comment | Organism |
|---|---|---|
| additional information | enhancement of L-tryptophan hydroxylation activity of L-phenylalanine 4-hydroxylase from Chromobacterium violaceum using information on the crystal structures of aromatic amino acid hydroxylases including TPH | Homo sapiens |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
- |
Homo sapiens |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | P17752 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | residue lying adjacent to substrate is F313, role of F313 in substrate specificity, residue is different from L-phenylalanine 4-hydroxylase | Homo sapiens | ? | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| L-tryptophan 5-hydroxylase | - |
Homo sapiens |
| TPH | - |
Homo sapiens |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| additional information | residue Y235 is involved in cofactor binding, residue is different from L-phenylalanine 4-hydroxylase | Homo sapiens |
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