Movement of the Biotin Carboxylase B-domain as a Result of ATP Binding
Open Access
- 1 May 2000
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 275 (21) , 16183-16190
- https://doi.org/10.1074/jbc.275.21.16183
Abstract
No abstract availableKeywords
This publication has 22 references indexed in Scilit:
- A diverse superfamily of enzymes with ATP‐dependent carboxylate—amine/thiol ligase activityProtein Science, 1997
- Vancomycin Resistance: Structure of D-Alanine:D-Alanine Ligase at 2.3 Å ResolutionScience, 1994
- Three-Dimensional Structure of the Biotin Carboxylase Subunit of Acetyl-CoA CarboxylaseBiochemistry, 1994
- Three-dimensional Structure of the Glutathione Synthetase from Escherichia coli B at 2·0 Å ResolutionJournal of Molecular Biology, 1993
- The genes encoding the two carboxyltransferase subunits of Escherichia coli acetyl-CoA carboxylase.Published by Elsevier ,1992
- Acetyl-CoA carboxylase from Escherichia coli: gene organization and nucleotide sequence of the biotin carboxylase subunit.Proceedings of the National Academy of Sciences, 1991
- FATTY ACID SYNTHESIS AND ITS REGULATIONAnnual Review of Biochemistry, 1983
- Acetyl-Coenzyme-A Carboxylase from Rat Liver. Subunit Structure and Proteolytic ModificationEuropean Journal of Biochemistry, 1975
- Acetyl Coenzyme A Carboxylase System of Escherichia coliJournal of Biological Chemistry, 1974
- Acetyl Coenzyme A Carboxylase* *The investigations cited in this review and unpublished studies carried out in the authors' laboratory were supported in part by research grants AM-14574 and AM-14575, United States Public Health Service and a research grant from the American Heart Association, Inc.Current Topics in Cellular Regulation, 1974