Home LiteratureArticle Details
PMID: 10064313 Published · ppublish English Journal Article Review

Molecular biology of biotin attachment to proteins.

The Journal of nutrition ·Vol. 129 ·No. 2S Suppl ·1999-00-00 ·Pages 477S-484S

Chapman-Smith A, Cronan JE

Abstract

Enzymatic attachment of biotin to proteins requires the interaction of a distinct domain of the acceptor protein (the "biotin domain") with the enzyme, biotin protein ligase, that catalyzes this essential and rare post-translational modification. Both biotin domains and biotin protein ligases are very strongly conserved throughout biology. This review concerns the protein structures and mechanisms involved in the covalent attachment of biotin to proteins.

MeSH Terms
Amino Acid Sequence Animals Bacteria/enzymology,metabolism Bacterial Proteins/chemistry,metabolism Biotin/biosynthesis,metabolism Biotinylation Carbon-Nitrogen Ligases/chemistry,metabolism Escherichia coli Proteins Humans Molecular Sequence Data Protein Binding Proteins/metabolism Repressor Proteins Sequence Alignment Transcription Factors
Chemicals
Bacterial Proteins Escherichia coli Proteins Proteins Repressor Proteins Transcription Factors Biotin Carbon-Nitrogen Ligases biotin carboxylase birA protein, E coli
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Chapman-Smith A
Department of Microbiology, University of Illinois, Urbana 61801, USA.
Cronan J E
Article Info
Journal
The Journal of nutrition
Abbr.
J Nutr
ISSN
0022-3166
Published
1999-00-00
Pages
477S-484S
Language
English
Region
United States
NLM ID
0404243
Subset
IM
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com