Regulatory properties of tetrahydrobiopterin cofactor bound at the active site of phenylalanine hydroxylase

Pteridines

Volumn 11, Issue 2, 2000, Pages 34-36

  Flatmark, T ^a   Erlandsen, H ^a   Bjorgo, E ^a   Solstad, T ^a   Doskeland, A P ^a   Stevens, R C ^a  

^a UNIVERSITY OF BERGEN   (Norway)

Author keywords

[No Author keywords available]

Indexed keywords

PHENYLALANINE 4 MONOOXYGENASE; TETRAHYDROBIOPTERIN;

CONFERENCE PAPER; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; CRYSTALLIZATION; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME PHOSPHORYLATION; ENZYME SUBSTRATE; PRIORITY JOURNAL; PROTEIN DOMAIN; RECEPTOR BINDING; SITE DIRECTED MUTAGENESIS;

EID: 0033777469     PISSN: 09334807     EISSN: 21954720     Source Type: Journal    
DOI: 10.1515/pteridines.2000.11.2.34     Document Type: Conference Paper

References (9)

1. The effect of ligands of phenylalanine 4-monooxygenase on the cAMP-dependent phosphorylation of the enzyme
2. Modulation by pterins of the phosphorylation and phenylalanine activation of phenylalanine 4-monooxygenase
3. Structural insight into the aromatic amino acid hydroxylases and their disease-related mutant forms
4. Structure/function relationships in human phenylalanine hydroxylase. Effect of terminal deletions on the oligomerization, activation and cooperativity of substrate binding to the enzyme
5. Partial characterization and three-dimesional-structural localization of eight mutations in exon 7 of the human phenylalanine hydroxylase gene associated with phenylketonuria
6. Crystal structure and site-specific mutagenesis of the pterin bound human phenylalanine hydroxylase
7. Crystal structure of the catalytic domain of human phenylalanine hydroxylase reveals the structural basis for phenylketonuria
8. The structural basis of the recognition of phenylalanine and pterin cofactors by phenylalanine hydroxylase: Implications for the catalytic mechanism
9. Structural basis of autoregulation of phenylalanine hydroxylase