The N-terminal domain of human holocarboxylase synthetase facilitates biotinylation via direct interaction with the substrate protein

FEBS Letters

Volumn 584, Issue 4, 2010, Pages 675-680

  Lee, Chung Kyung ^a,b   Cheong, Chaejoon ^a,b   Jeon, Young Ho ^a,b  

^a Korea Basic Science Institute (KBSI)   (South Korea)

^b University of Science and Technology (UST)   (South Korea)

Author keywords

Acetyl CoA carboxylase; Avidin blot; Biotinoyl domain; Biotinylation; Holocarboxylase synthetase

Indexed keywords

HOLOCARBOXYLASE SYNTHETASE; SYNTHETASE; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; BIOTINYLATION; CATALYSIS; ENZYME ACTIVITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; MOLECULAR RECOGNITION; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; STRUCTURE ANALYSIS;

BINDING SITES; BIOTINYLATION; CARBON-NITROGEN LIGASES; CATALYTIC DOMAIN; CHYMOTRYPSIN; CIRCULAR DICHROISM; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENDOPEPTIDASE K; HUMANS; MAGNETIC RESONANCE SPECTROSCOPY; MUTATION; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; SUBSTRATE SPECIFICITY; SUBTILISIN;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 77649270119     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2009.12.059     Document Type: Article

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