Enzyme

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     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:1.14.16.1
Description:Phenylalanine 4-monooxygenase.
Alternative Name: Phenylalanine hydroxylase.
Phenylalanine 4-hydroxylase.
Phenylalaninase.
PAH.
Prosite: PDOC00316;
PDB:
PDBScop
5J6D 8031297; 8043675; 8031297; 8043675;
5TPG 8031297; 8043675;
5L01 8031297; 8043675;
3HFB 8031297; 8043675;
3HF8 8031297; 8043675;
 » show all

Cath: 1.10.800.10; 3.30.70.260;

3D structure

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References

External Links

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:

1.14.16.1;

Phylogenetic Tree:

1.14.16.1;

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

References

TitleAuthorsDatePubMed ID
Mechanism of metal-independent hydroxylation by Chromobacterium violaceum phenylalanine hydroxylase.Carr RT, Balasubramanian S, Hawkins PC, Benkovic SJ1995 Jun 67779797
Phenylalanine hydroxylase from Chromobacterium violaceum is a copper-containing monooxygenase. Kinetics of the reductive activation of the enzyme.Pember SO, Villafranca JJ, Benkovic SJ1986 Oct 213024714
Direct evidence for a phenylalanine site in the regulatory domain of phenylalanine hydroxylase.Li J, Ilangovan U, Daubner SC, Hinck AP, Fitzpatrick PF2011 Jan 1520951114
Anabolic function of phenylalanine hydroxylase in Caenorhabditis elegans.Calvo AC, Pey AL, Ying M, Loer CM, Martinez A2008 Aug18460651
Insights into the catalytic mechanisms of phenylalanine and tryptophan hydroxylase from kinetic isotope effects on aromatic hydroxylation.Pavon JA, Fitzpatrick PF2006 Sep 1216953590
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 KU2006 Oct16935936
Order of substrate binding in bacterial phenylalanine hydroxylase and its mechanistic implication for pterin-dependent oxygenases.Volner A, Zoidakis J, Abu-Omar MM2003 Jan12459906
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 T2003 Feb 112379147
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 E2002 Jul 2612126628
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 RC2002 Jul 1212096915
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 E2001 Nov 2311718561