The polypeptide Syn67 interacts physically with human holocarboxylase synthetase, but is not a target for biotinylation

Archives of Biochemistry and Biophysics

Volumn 495, Issue 1, 2010, Pages 35-41

  Hassan, Yousef I ^a   Moriyama, Hideaki ^a   Zempleni, Janos ^a  

^a UNIVERSITY OF NEBRASKA LINCOLN   (United States)

Author keywords

Biotin; Domains; Holocarboxylase synthetase; Substrate; Syn67

Indexed keywords

ARGININE; GLYCINE; HISTONE; HOLOCARBOXYLASE SYNTHETASE; LYSINE; POLYPEPTIDE; PROTEIN SYN67; SYNTHETASE; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; BINDING SITE; BIOTINYLATION; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ENZYME ACTIVITY; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION;

AMINO ACID SEQUENCE; BINDING SITES; BIOTINYLATION; CARBON-NITROGEN LIGASES; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; MUTATION; PEPTIDES; SUBSTRATE SPECIFICITY;

EID: 76849097764     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2009.12.017     Document Type: Article

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