Carboxyl transferase domain
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| 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 | ||||||||
| SCOP2 | 1od2 / SCOPe / SUPFAM | ||||||||
| 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 use 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. doi:10.1128/JB.175.17.5301-5308.1993. PMC 206582. PMID 8366018.