The Distinct N-termini of Two Human Hcs Isoforms Influence Biotin Acceptor Substrate Recognition
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چکیده
THE DISTINCT N-TERMINI OF TWO HUMAN HCS ISOFORMS INFLUENCE BIOTIN ACCEPTOR SUBSTRATE RECOGNITION Maria Ingaramo and Dorothy Beckett From the Department of Chemistry and Biochemistry, Center for Biological Structure and Organization, University of Maryland, College Park, MD 20742 Running title: Interaction of HCS isoforms with acceptor protein substrate *Address correspondence to: Dorothy Beckett, Department of Chemistry and Biochemistry, University of Maryland, College Park, MD 20742, telephone: 301-405-1812, fax: 301-314-9121, e-mail: [email protected]
منابع مشابه
N- and C-terminal domains in human holocarboxylase synthetase participate in substrate recognition.
Holocarboxylase synthetase (HCS) catalyzes the binding of the vitamin biotin to carboxylases and histones. Carboxylases mediate essential steps in macronutrient metabolism. For example, propionyl-CoA carboxylase (PCC) catalyzes the carboxylation of propionyl-CoA in the metabolism of odd-chain fatty acids. HCS comprises four putative domains, i.e., the N-terminus, the biotin transfer/ATP-binding...
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