Disulfide-linked dimers of human adrenaline synthesizing enzyme PNMT are catalytically active

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1750, Issue 1, 2005, Pages 82-92

  Gee, Christine L ^a   Nourse, Amanda ^a,d   Hsin, A Yen ^a   Wu, Qian ^b   Tyndall, Joel D ^a,e   Grunewald, Gary L ^c   McLeish, Michael J ^b   Martin, Jennifer L ^a  

^a UNIVERSITY OF QUEENSLAND   (Australia)

^b UNIVERSITY OF MICHIGAN   (United States)

^c UNIVERSITY OF KANSAS   (United States)

^d ST JUDE CHILDREN S RESEARCH HOSPITAL   (United States)

^e UNIVERSITY OF OTAGO   (New Zealand)

Author keywords

Analytical ultracentrifugation; Catalytic activity; Catecholamine synthesis; Chromatography; Dimerisation; Disulfide bond formation; Protein purification

Indexed keywords

DIMER; DISULFIDE; MONOMER; OLIGOMER; PHENYLETHANOLAMINE N METHYLTRANSFERASE; PROTEIN; REDUCING AGENT;

ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; CRYSTALLIZATION; DISULFIDE BOND; ENZYME ACTIVITY; ENZYME MECHANISM; MUTANT; NONHUMAN; PRIORITY JOURNAL; WILD TYPE;

BINDING SITES; CATALYSIS; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; CYSTEINE; DIMERIZATION; DISULFIDES; DITHIOTHREITOL; HUMANS; MODELS, MOLECULAR; PHENYLETHANOLAMINE N-METHYLTRANSFERASE; PROTEIN CONFORMATION; REDUCING AGENTS; SOLUTIONS; ULTRACENTRIFUGATION;

EID: 20444391761     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2005.03.006     Document Type: Article

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