Carboxybiotin decarboxylase
Carboxybiotin decarboxylase (EC 7.2.4.1, MadB, carboxybiotin protein decarboxylase) is an enzyme with systematic name carboxybiotinyl-(protein) carboxy-lyase.[1][2] This enzyme catalyses the following chemical reaction
- a carboxybiotinyl-[protein] + n Na+in + H+out CO2 + a biotinyl-[protein] + n Na+out (n = 1--2)
| Carboxybiotin decarboxylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 7.2.4.1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
This enzyme is an integral membrane protein MadB from the anaerobic bacterium Malonomonas rubra.
References
- Berg M, Hilbi H, Dimroth P (April 1997). "Sequence of a gene cluster from Malonomonas rubra encoding components of the malonate decarboxylase Na+ pump and evidence for their function". European Journal of Biochemistry. 245 (1): 103–15. doi:10.1111/j.1432-1033.1997.00103.x. PMID 9128730.
- Dimroth P, Hilbi H (July 1997). "Enzymic and genetic basis for bacterial growth on malonate". Molecular Microbiology. 25 (1): 3–10. doi:10.1046/j.1365-2958.1997.4611824.x. PMID 11902724.
External links
- Carboxybiotin+decarboxylase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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