Biotin-independent malonate decarboxylase
| Biotin-independent malonate decarboxylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.1.1.88 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Biotin-independent malonate decarboxylase (EC 4.1.1.88, malonate decarboxylase (without biotin), malonate decarboxylase, MDC) is an enzyme with systematic name malonate carboxy-lyase (biotin-independent).[1][2][3][4][5][6][7][8][9] This enzyme catalyses the following chemical reaction
Two types of malonate decarboxylase are currently known, both of which form multienzyme complexes.
References
- ^ Schmid, M.; Berg, M.; Hilbi, H.; Dimroth, P. (1996). "Malonate decarboxylase of Klebsiella pneumoniae catalyses the turnover of acetyl and malonyl thioester residues on a coenzyme-A-like prosthetic group". Eur. J. Biochem. 237: 221–228. doi:10.1111/j.1432-1033.1996.0221n.x. PMID 8620876.
- ^ Byun, H.S.; Kim, Y.S. (1997). "Subunit organization of bacterial malonate decarboxylases: the smallest δ subunit as an acyl-carrier protein". J. Biochem. Mol. Biol. 30: 132–137.
- ^ Hoenke, S.; Schmid, M.; Dimroth, P. (1997). "Sequence of a gene cluster from Klebsiella pneumoniae encoding malonate decarboxylase and expression of the enzyme in Escherichia coli". Eur. J. Biochem. 246: 530–538. doi:10.1111/j.1432-1033.1997.00530.x. PMID 9208947.
- ^ Chohnan, S.; Fujio, T.; Takaki, T.; Yonekura, M.; Nishihara, H.; Takamura, Y. (1998). "Malonate decarboxylase of Pseudomonas putida is composed of five subunits". FEMS Microbiol. Lett. 169: 37–43. doi:10.1111/j.1574-6968.1998.tb13296.x. PMID 9851033.
- ^ Hoenke, S.; Schmid, M.; Dimroth, P. (2000). "Identification of the active site of phosphoribosyl-dephospho-coenzyme A transferase and relationship of the enzyme to an ancient class of nucleotidyltransferases". Biochemistry. 39: 13233–13240. doi:10.1021/bi001154u. PMID 11052676.
- ^ Handa, S.; Koo, J.H.; Kim, Y.S.; Floss, H.G. (1999). "Stereochemical course of biotin-independent malonate decarboxylase catalysis". Arch. Biochem. Biophys. 370: 93–96. doi:10.1006/abbi.1999.1369. PMID 10496981.
- ^ Koo, J.H.; Kim, Y.S. (1999). "Functional evaluation of the genes involved in malonate decarboxylation by Acinetobacter calcoaceticus". Eur. J. Biochem. 266: 683–690. doi:10.1046/j.1432-1327.1999.00924.x. PMID 10561613.
- ^ Kim, Y.S. (2002). "Malonate metabolism: biochemistry, molecular biology, physiology, and industrial application". J. Biochem. Mol. Biol. 35: 443–451. doi:10.5483/bmbrep.2002.35.5.443. PMID 12359084.
- ^ Dimroth, P.; Hilbi, H. (1997). "Enzymic and genetic basis for bacterial growth on malonate". Mol. Microbiol. 25: 3–10. doi:10.1046/j.1365-2958.1997.4611824.x. PMID 11902724.
External links
- Biotin-independent+malonate+decarboxylase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)