Journal of Nutrition OpenSOurce Diets- www.ResearchDiets.com

Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
 QUICK SEARCH:   [advanced]


     


J. Nutr. First published December 4, 2008; doi:10.3945/jn.108.095760
Journal of Nutrition, doi:10.3945/jn.108.095760
Vol. 139, No. 1, 167-170, January 2009

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
139/1/167    most recent
jn.108.095760v1
Right arrow Purchase Article
Right arrow View Shopping Cart
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Beckett, D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Beckett, D.
© 2009 American Society for Nutrition


Symposium: Advances in Understanding of the Biological Role of Biotin at the Clinical, Biochemical, and Molecular Level

Biotin Sensing at the Molecular Level1–3,

Dorothy Beckett*

Department of Chemistry and Biochemistry, College of Chemical and Life Sciences, University of Maryland, College Park, MD 20742

Biotin influences transcription in organisms from bacteria to humans. The enzyme, biotin protein ligase, which catalyzes post-transcriptional biotin addition to biotin-dependent carboxylases, plays a central roll in transmitting the demand for biotin to gene expression. The molecular mechanism of this communication in bacteria is well understood and involves competing protein:protein interactions. Biochemical measurements indicate that this competition is kinetically controlled. In humans, the biochemistry of biotin sensing at the transcriptional level is not well characterized. However, the biotin holoenzyme ligase (holocarboxylase synthetase) is proposed to both catalyze biotin addition to carboxylases and to histones in its metabolic and transcriptional roles, respectively. Control of human holocarboxylase synthetase function is, however, considerably more complex than the simple competitive protein protein interactions observed in bacterial systems.


* To whom correspondence should be addressed. E-mail: dbeckett{at}umd.edu.

Published online 3 December 2008.







Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Copyright © 2009 by American Society for Nutrition