A Four-Cysteine Zinc Finger in Carboxyltransferase Structurally Links the Functions of Enzymatic Activity and Negative Feedback Regulation of Translation
Acetyl-CoA carboxylase is the first and committed step of de novo fatty acid synthesis in all organisms. In Escherichia coli, the enzyme is expressed as separate proteins for the three functional components: a biotin carboxylase, a biotin carboxyl carrier protein, and a carboxyltransferase. The carb...
Main Author: | Meades, Glen D. |
---|---|
Other Authors: | Waldrop, Grover |
Format: | Others |
Language: | en |
Published: |
LSU
2010
|
Subjects: | |
Online Access: | http://etd.lsu.edu/docs/available/etd-08112010-140057/ |
Similar Items
-
The Role of Cysteine 230 and Lysine 238 of Biotin Carboxylase in the Deprotonation of Biotin and Synthesis of a Bisubstrate Analog Inhibitor of Carboxyltransferase
by: Levert, Keith Logan
Published: (2002) -
The role of symmetry in the regulation of bacterial carboxyltransferase
by: Waldrop Grover L.
Published: (2011-04-01) -
Inhibition and Nucleic Acid Binding Studies of the Carboxyltransferase Component of Bacterial Acetyl-CoA Carboxylase
by: Benson, Brian
Published: (2011) -
The 17 KDa Protein in Photosystem II, Purification and Interaction with the Photosystem
by: Meades, Glen
Published: (2005) -
The ABC of KRAB zinc finger proteins
by: Looman, Camilla
Published: (2003)