Biotin-independent malonate decarboxylase
Appearance
(Redirected from EC 4.1.1.88)
Biotin-independent malonate decarboxylase | |||||||||
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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 | ||||||||
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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
[edit]- ^ Schmid M, Berg M, Hilbi H, Dimroth P (April 1996). "Malonate decarboxylase of Klebsiella pneumoniae catalyses the turnover of acetyl and malonyl thioester residues on a coenzyme-A-like prosthetic group". European Journal of Biochemistry. 237 (1): 221–8. 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 (June 1997). "Sequence of a gene cluster from Klebsiella pneumoniae encoding malonate decarboxylase and expression of the enzyme in Escherichia coli". European Journal of Biochemistry. 246 (2): 530–8. doi:10.1111/j.1432-1033.1997.00530.x. PMID 9208947.
- ^ Chohnan S, Fujio T, Takaki T, Yonekura M, Nishihara H, Takamura Y (December 1998). "Malonate decarboxylase of Pseudomonas putida is composed of five subunits". FEMS Microbiology Letters. 169 (1): 37–43. doi:10.1111/j.1574-6968.1998.tb13296.x. PMID 9851033.
- ^ Hoenke S, Schmid M, Dimroth P (October 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 (43): 13233–40. doi:10.1021/bi001154u. PMID 11052676.
- ^ Handa S, Koo JH, Kim YS, Floss HG (October 1999). "Stereochemical course of biotin-independent malonate decarboxylase catalysis". Archives of Biochemistry and Biophysics. 370 (1): 93–6. doi:10.1006/abbi.1999.1369. PMID 10496981.
- ^ Koo JH, Kim YS (December 1999). "Functional evaluation of the genes involved in malonate decarboxylation by Acinetobacter calcoaceticus". European Journal of Biochemistry. 266 (2): 683–90. doi:10.1046/j.1432-1327.1999.00924.x. PMID 10561613.
- ^ Kim YS (September 2002). "Malonate metabolism: biochemistry, molecular biology, physiology, and industrial application". Journal of Biochemistry and Molecular Biology. 35 (5): 443–51. doi:10.5483/bmbrep.2002.35.5.443. PMID 12359084.
- ^ 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
[edit]- Biotin-independent+malonate+decarboxylase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)