PKU mutation (D143G) associated with an apparent high residual enzyme activity: Expression of a kinetic variant form of phenylalanine hydroxylase in three different systems

Human Mutation

Volumn 8, Issue 3, 1996, Pages 236-246

  Knappskog, Per M ^a   Eiken, Hans Geir ^a   Martínez, Aurora ^a   Bruland, Ove ^a   Apold, Jaran ^a   Flatmark, Torgeir ^a  

^a UNIVERSITY OF BERGEN   (Norway)

Author keywords

D143G mutation; Enzyme kinetics; Expression systems; Phenylalanine hydroxylase; Phenylketonuria; Substrate affinity; Substrate inhibition

Indexed keywords

PHENYLALANINE 4 MONOOXYGENASE; RECOMBINANT PHENYLALANINE 4 MONOOXYGENASE; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; ENZYME ANALYSIS; ENZYME KINETICS; ENZYME STABILITY; ESCHERICHIA COLI; GENE FUSION; GENE MUTATION; HUMAN; HUMAN CELL; HYDROXYLATION; PHENOTYPE; PHENYLKETONURIA; PHYSICAL CHEMISTRY; PRIORITY JOURNAL; PROTEIN EXPRESSION;

ASPARTIC ACID; CELL LINE; CLONING, MOLECULAR; ESCHERICHIA COLI; EXONS; GLYCINE; HUMANS; KIDNEY; KINETICS; MUTAGENESIS, SITE-DIRECTED; PHENYLALANINE HYDROXYLASE; PHENYLKETONURIAS; POLYMERASE CHAIN REACTION; RECOMBINANT FUSION PROTEINS; VARIATION (GENETICS);

EID: 0029796673     PISSN: 10597794     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1098-1004(1996)8:3<236::AID-HUMU7>3.0.CO;2-7     Document Type: Article

References (8)

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