EC Tree |
1. Oxidoreductases |
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen |
1.14.16 With reduced pteridine as one donor, and incorporation of one atom of oxygen into the other donor |
ID: | 1.14.16.4 | ||
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Description: | Tryptophan 5-monooxygenase. | ||
Alternative Name: |
Tryptophan hydroxylase. Tryptophan 5-hydroxylase. L-tryptophan hydroxylase. Indoleacetic acid-5-hydroxylase. | ||
Prosite: | PDOC00316; | ||
PDB: |
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Cath: | 1.10.800.10; |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.UniProtKB Enzyme Link: | UniProtKB 1.14.16.4 |
BRENDA Enzyme Link: | BRENDA 1.14.16.4 |
KEGG Enzyme Link: | KEGG1.14.16.4 |
BioCyc Enzyme Link: | BioCyc 1.14.16.4 |
ExPASy Enzyme Link: | ExPASy1.14.16.4 |
EC2PDB Enzyme Link: | EC2PDB 1.14.16.4 |
ExplorEnz Enzyme Link: | ExplorEnz 1.14.16.4 |
PRIAM enzyme-specific profiles Link: | PRIAM 1.14.16.4 |
IntEnz Enzyme Link: | IntEnz 1.14.16.4 |
MEDLINE Enzyme Link: | MEDLINE 1.14.16.4 |
MSA: | |
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Phylogenetic Tree: | |
Uniprot: | |
M-CSA: |
RHEA:16709 | (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-tryptophan + O2 = (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin + 5-hydroxy-L-tryptophan |
RULE(radius=1) | [*:1]-[CH;+0:2](-[*:3])-[*:4].[*:5]:[cH;+0:6]:[*:7].[O;H0;+0:8]=[O;H0;+0:9]>>[*:1]-[C;H0;+0:2](-[*:3])(-[*:4])-[OH;+0:8].[*:5]:[c;H0;+0:6](:[*:7])-[OH;+0:9] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
Title | Authors | Date | PubMed ID |
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Purification and some properties of bovine pineal tryptophan 5-monooxygenase. | Nukiwa T, Toyama C, Okita C, Kataoka T, Ichiyama A | 1974 Oct 8 | 4429558 |
Three-dimensional structure of human tryptophan hydroxylase and its implications for the biosynthesis of the neurotransmitters serotonin and melatonin. | Wang L, Erlandsen H, Haavik J, Knappskog PM, Stevens RC | 2002 Oct 22 | 12379098 |
Influence of steric bulk and electrostatics on the hydroxylation regiospecificity of tryptophan hydroxylase: characterization of methyltryptophans and azatryptophans as substrates. | Moran GR, Phillips RS, Fitzpatrick PF | 1999 Dec 7 | 10587452 |