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 |
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5J6D;
5TPG;
5L01;
3HFB;
3HF8;
3HF6;
1MLW;
4Q3Z;
4Q3Y;
4Q3X;
4Q3W;
4JPY;
4JPX;
4ETL;
4ESM;
3TK4;
3TK2;
3TCY;
1LTZ;
1LTV;
1LTU;
6N1K;
2PAH;
6PAH;
5PAH;
4PAH;
4ANP;
3PAH;
1TG2;
1TDW;
1PAH;
1MMT;
1MMK;
1LRM;
1J8T;
1DMW;
2TOH;
1TOH;
5FGJ;
5EGQ;
5DEN;
2PHM;
1PHZ;
5JK8;
5JK6;
5JK5;
4V06;
3E2T;
2XSN;
1KW0;
1J8U;
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UniProtKB Enzyme Link: | UniProtKB 1.14.16.1 |
BRENDA Enzyme Link: | BRENDA 1.14.16.1 |
KEGG Enzyme Link: | KEGG1.14.16.1 |
BioCyc Enzyme Link: | BioCyc 1.14.16.1 |
ExPASy Enzyme Link: | ExPASy1.14.16.1 |
EC2PDB Enzyme Link: | EC2PDB 1.14.16.1 |
ExplorEnz Enzyme Link: | ExplorEnz 1.14.16.1 |
PRIAM enzyme-specific profiles Link: | PRIAM 1.14.16.1 |
IntEnz Enzyme Link: | IntEnz 1.14.16.1 |
MEDLINE Enzyme Link: | MEDLINE 1.14.16.1 |
MSA: | |
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Phylogenetic Tree: | |
Uniprot: | |
M-CSA: |
RHEA:20273 | (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-phenylalanine + O2 = (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin + L-tyrosine |
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 |
---|---|---|---|
Mechanism of metal-independent hydroxylation by Chromobacterium violaceum phenylalanine hydroxylase. | Carr RT, Balasubramanian S, Hawkins PC, Benkovic SJ | 1995 Jun 6 | 7779797 |
Phenylalanine hydroxylase from Chromobacterium violaceum is a copper-containing monooxygenase. Kinetics of the reductive activation of the enzyme. | Pember SO, Villafranca JJ, Benkovic SJ | 1986 Oct 21 | 3024714 |
Direct evidence for a phenylalanine site in the regulatory domain of phenylalanine hydroxylase. | Li J, Ilangovan U, Daubner SC, Hinck AP, Fitzpatrick PF | 2011 Jan 15 | 20951114 |
Anabolic function of phenylalanine hydroxylase in Caenorhabditis elegans. | Calvo AC, Pey AL, Ying M, Loer CM, Martinez A | 2008 Aug | 18460651 |
Insights into the catalytic mechanisms of phenylalanine and tryptophan hydroxylase from kinetic isotope effects on aromatic hydroxylation. | Pavon JA, Fitzpatrick PF | 2006 Sep 12 | 16953590 |
Specific interaction of the diastereomers 7(R)- and 7(S)-tetrahydrobiopterin with phenylalanine hydroxylase: implications for understanding primapterinuria and vitiligo. | Pey AL, Martinez A, Charubala R, Maitland DJ, Teigen K, Calvo A, Pfleiderer W, Wood JM, Schallreuter KU | 2006 Oct | 16935936 |
Order of substrate binding in bacterial phenylalanine hydroxylase and its mechanistic implication for pterin-dependent oxygenases. | Volner A, Zoidakis J, Abu-Omar MM | 2003 Jan | 12459906 |
Substrate-induced conformational transition in human phenylalanine hydroxylase as studied by surface plasmon resonance analyses: the effect of terminal deletions, substrate analogues and phosphorylation. | Stokka AJ, Flatmark T | 2003 Feb 1 | 12379147 |
Crystal structure of the ternary complex of the catalytic domain of human phenylalanine hydroxylase with tetrahydrobiopterin and 3-(2-thienyl)-L-alanine, and its implications for the mechanism of catalysis and substrate activation. | Andersen OA, Flatmark T, Hough E | 2002 Jul 26 | 12126628 |
Structural comparison of bacterial and human iron-dependent phenylalanine hydroxylases: similar fold, different stability and reaction rates. | Erlandsen H, Kim JY, Patch MG, Han A, Volner A, Abu-Omar MM, Stevens RC | 2002 Jul 12 | 12096915 |
High resolution crystal structures of the catalytic domain of human phenylalanine hydroxylase in its catalytically active Fe(II) form and binary complex with tetrahydrobiopterin. | Andersen OA, Flatmark T, Hough E | 2001 Nov 23 | 11718561 |