Posttranslational hydroxylation of human phenylalanine hydroxylase is a novel example of enzyme self-repair within the second coordination sphere of catalytic iron

Journal of the American Chemical Society

Volumn 125, Issue 16, 2003, Pages 4710-4711

  Kinzie, Sylvia Daoud ^a   Thevis, Mario ^a,b   Ngo, Khanh ^a   Whitelegge, Julian ^a   Loo, Joseph A ^a,b   Abu Omar, Mahdi M ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PHENYLALANINE 4 MONOOXYGENASE;

ARTICLE; BINDING AFFINITY; CHROMOBACTERIUM; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME ISOLATION; ENZYME KINETICS; ENZYME MODIFICATION; ENZYME STABILITY; ENZYME STRUCTURE; HYDROXYLATION; MASS SPECTROMETRY; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; OLIGOMERIZATION; PROTEIN PROCESSING; THERMOSTABILITY; WILD TYPE;

AMINO ACID SEQUENCE; ENZYME STABILITY; HUMANS; HYDROGEN BONDING; HYDROXYLATION; MASS SPECTROMETRY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NONHEME IRON PROTEINS; PHENYLALANINE HYDROXYLASE; POINT MUTATION; PROTEIN CONFORMATION; PROTEIN PROCESSING, POST-TRANSLATIONAL;

EID: 0037462093     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja034452y     Document Type: Article

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