Flavinylation and assembly of succinate dehydrogenase are dependent on the C-terminal tail of the flavoprotein subunit

Journal of Biological Chemistry

Volumn 287, Issue 48, 2012, Pages 40670-40679

  Kim, Hyung J ^a   Jeong, Mi Young ^a   Na, Un ^a   Winge, Dennis R ^a  

^a UNIVERSITY OF UTAH HEALTH SCIENCES CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ARG RESIDUES; ARGININE RESIDUE; C-TERMINAL TAIL; COVALENT ATTACHMENT; ENZYMATIC FUNCTIONS; FLAVINYLATION; MEMBRANE ANCHORS; MUTANT CELLS; STEADY-STATE LEVEL; SUCCINATE DEHYDROGENASE; TETRAMERIC ENZYMES; TETRAMERS;

AMINO ACIDS; OLIGOMERS;

ASSOCIATION REACTIONS;

ARGININE; CYSTEINE; DNA; FLAVOPROTEIN; POLYPEPTIDE; SUCCINATE DEHYDROGENASE; TETRAMER;

ANALYTIC METHOD; ARTICLE; BINDING SITE; CARBOXY TERMINAL SEQUENCE; DNA SEQUENCE; ENZYME ACTIVITY; FLAVINYLATION; GENE LOCUS; GENE MUTATION; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN SUBUNIT; SACCHAROMYCES CEREVISIAE; STEADY STATE; YEAST;

BINDING SITES; FLAVINS; FLAVOPROTEINS; HUMANS; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, TERTIARY; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SUCCINATE DEHYDROGENASE;

EID: 84870012890     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.405704     Document Type: Article

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