Natural phenylalanine hydroxylase variants that confer a mild phenotype affect the enzyme's conformational stability and oligomerization equilibrium

Biochimica et Biophysica Acta - Molecular Basis of Disease

Volumn 1812, Issue 11, 2011, Pages 1435-1445

  Cerreto, Monica ^a   Cavaliere, Paola ^a,b   Carluccio, Carla ^a,b   Amato, Felice ^a   Zagari, Adriana ^a,b   Daniele, Aurora ^a,b,c   Salvatore, Francesco ^a,b,d  

^a CEINGE BIOTECNOLOGIE AVANZATE   (Italy)

^b UNIVERSITY OF NAPLES FEDERICO II   (Italy)

^c SECOND UNIVERSITY OF NAPLES   (Italy)

^d IRCCS SDN   (Italy)

Author keywords

BH4 responsiveness; Hyperphenylalaninemia; Number and brightness; PAH conformational stability; PAH oligomerization equilibrium; Phenylalanine hydroxylase

Indexed keywords

MUTANT PROTEIN; PHENYLALANINE 4 MONOOXYGENASE;

ARTICLE; CIRCULAR DICHROISM; CONFOCAL MICROSCOPY; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME INACTIVATION; ENZYME OLIGOMERIZATION; ENZYME STABILITY; FEMALE; GEL PERMEATION CHROMATOGRAPHY; HELA CELL; HUMAN; HUMAN CELL; IN VIVO STUDY; LIGHT SCATTERING; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; PROTEIN VARIANT; SITE DIRECTED MUTAGENESIS; THERMOSTABILITY; WILD TYPE;

BIOPTERIN; CIRCULAR DICHROISM; ENZYME STABILITY; HELA CELLS; HUMANS; IMMUNOBLOTTING; MUTAGENESIS, SITE-DIRECTED; MUTATION; PHENOTYPE; PHENYLALANINE HYDROXYLASE; PHENYLKETONURIAS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN MULTIMERIZATION;

EID: 80053448573     PISSN: 09254439     EISSN: 1879260X     Source Type: Journal    
DOI: 10.1016/j.bbadis.2011.07.012     Document Type: Article

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