Visualization of PLP-bound intermediates in hemeless variants of human cystathionine β-synthase: Evidence that lysine 119 is a general base

Archives of Biochemistry and Biophysics

Volumn 427, Issue 2, 2004, Pages 188-196

  Evande, Ruby ^a   Ojha, Sunil ^a,b   Banerjee, Ruma ^a  

^a UNIVERSITY OF NEBRASKA LINCOLN   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Cystathionine; Cystathionine synthase; Homocysteine; Pyridoxal phosphate

Indexed keywords

CYSTATHIONINE; CYSTATHIONINE BETA SYNTHASE; HOMOCYSTEINE; ISOPROTEIN; LYSINE; PYRIDOXAL 5 PHOSPHATE; SCHIFF BASE;

ADDITION REACTION; AMINO TERMINAL SEQUENCE; ARTICLE; CATALYSIS; ENZYME ISOLATION; PRIORITY JOURNAL; PROTEIN ENGINEERING; PROTEIN FOLDING; PROTEIN STRUCTURE; PROTEIN VARIANT; PROTON TRANSPORT; STRUCTURE ANALYSIS;

BINDING SITES; CYSTATHIONINE BETA-SYNTHASE; ENZYME ACTIVATION; HEME; HUMANS; LYSINE; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MUTATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; PYRIDOXAL PHOSPHATE; RECOMBINANT PROTEINS; SPECTROPHOTOMETRY, ULTRAVIOLET; STEREOISOMERISM; VARIATION (GENETICS);

EID: 2942542787     PISSN: 00039861     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.abb.2004.04.027     Document Type: Article

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