Carboxyl transferase domain
| Carboxyl_trans | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 crystal structure of the carboxyltransferase subunit of the bacterial ion pump glutaconyl-coenzyme a decarboxylase | |||||||||
| Identifiers | |||||||||
| Symbol | Carboxyl_trans | ||||||||
| Pfam | PF01039 | ||||||||
| Pfam clan | CL0127 | ||||||||
| InterPro | IPR000022 | ||||||||
| SCOP | 1od2 | ||||||||
| SUPERFAMILY | 1od2 | ||||||||
| TCDB | 3.B.1 | ||||||||
| |||||||||
In molecular biology, proteins containing the carboxyl transferase domain include biotin-dependent carboxylases.[1][2] This domain carries out the following reaction: transcarboxylation from biotin to an acceptor molecule. There are two recognised types of carboxyl transferase. One of them uses acyl-CoA and the other uses 2-oxo acid as the acceptor molecule of carbon dioxide. All of the members in this family utilise acyl-CoA as the acceptor molecule.
References
- ↑ Toh H, Kondo H, Tanabe T (August 1993). "Molecular evolution of biotin-dependent carboxylases". Eur. J. Biochem. 215 (3): 687–96. doi:10.1111/j.1432-1033.1993.tb18080.x. PMID 8102604.
- ↑ Thornton CG, Kumar GK, Haase FC, Phillips NF, Woo SB, Park VM, Magner WJ, Shenoy BC, Wood HG, Samols D (September 1993). "Primary structure of the monomer of the 12S subunit of transcarboxylase as deduced from DNA and characterization of the product expressed in Escherichia coli". J. Bacteriol. 175 (17): 5301–8. PMC 206582
. PMID 8366018.
This article incorporates text from the public domain Pfam and InterPro IPR000022
This article is issued from Wikipedia - version of the 5/28/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.