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{{Infobox enzyme
| Name = Biotin-independent malonate decarboxylase
| EC_number = 4.1.1.88
| CAS_number = 
| IUBMB_EC_number = 4/1/1/88
| GO_code = 
| image = 
| width = 
| caption =
}}
'''Biotin-independent malonate decarboxylase''' ({{EC number|4.1.1.88}}, ''malonate decarboxylase (without biotin)'', ''malonate decarboxylase'', ''MDC'') is an [[enzyme]] with system name ''malonate carboxy-lyase (biotin-independent)''.<ref>{{cite journal | title = Malonate decarboxylase of ''Klebsiella pneumoniae'' catalyses the turnover of acetyl and malonyl thioester residues on a coenzyme-A-like prosthetic  group |author = Schmid, M., Berg, M., Hilbi, H. and Dimroth, P. |journal = Eur. J. Biochem. |year = 1996 |volume = 237 |pages = 221–228 |pmid = 8620876}}</ref><ref>{{cite journal | title = Subunit organization of bacterial malonate decarboxylases: the smallest &delta; subunit as an acyl-carrier protein |author = Byun, H.S. and Kim, Y.S. |journal = J. Biochem. Mol. Biol. |year = 1997 |volume = 30 |pages = 132–137 |pmid = }}</ref><ref>{{cite journal | title = Sequence of a gene cluster from ''Klebsiella pneumoniae'' encoding malonate decarboxylase and expression of the enzyme in ''Escherichia coli'' |author = Hoenke, S., Schmid, M. and Dimroth, P. |journal = Eur. J. Biochem. |year = 1997 |volume = 246 |pages = 530–538 |pmid = 9208947}}</ref><ref>{{cite journal | title = Malonate decarboxylase of ''Pseudomonas putida'' is composed of five subunits |author = Chohnan, S., Fujio, T., Takaki, T., Yonekura, M., Nishihara, H. and Takamura, Y. |journal = FEMS Microbiol. Lett. |year = 1998 |volume = 169 |pages = 37–43 |pmid = 9851033}}</ref><ref>{{cite journal | title = Identification of the active site of phosphoribosyl-dephospho-coenzyme A transferase and relationship of the enzyme to an ancient class of  nucleotidyltransferases |author = Hoenke, S., Schmid, M. and Dimroth, P. |journal = Biochemistry |year = 2000 |volume = 39 |pages = 13233–13240 |pmid = 11052676}}</ref><ref>{{cite journal | title = Stereochemical course of biotin-independent malonate decarboxylase catalysis |author = Handa, S., Koo, J.H., Kim, Y.S. and Floss, H.G. |journal = Arch. Biochem. Biophys. |year = 1999 |volume = 370 |pages = 93–96 |pmid = 10496981}}</ref><ref>{{cite journal | title = Functional evaluation of the genes involved in malonate decarboxylation by ''Acinetobacter calcoaceticus'' |author = Koo, J.H. and Kim, Y.S. |journal = Eur. J. Biochem. |year = 1999 |volume = 266 |pages = 683–690 |pmid = 10561613}}</ref><ref>{{cite journal | title = Malonate metabolism: biochemistry, molecular biology, physiology, and industrial application |author = Kim, Y.S. |journal = J. Biochem. Mol. Biol. |year = 2002 |volume = 35 |pages = 443–451 |pmid = 12359084}}</ref><ref>{{cite journal | title = Enzymic and genetic basis for bacterial growth on malonate |author = Dimroth, P. and Hilbi, H. |journal = Mol. Microbiol. |year = 1997 |volume = 25 |pages = 3–10 |pmid = 11902724}}</ref> This enzyme [[catalysis|catalyses]] the following [[chemical reaction]]

: [[malonate]] + H<sup>+</sup> <math>\rightleftharpoons</math> [[acetate]] + CO<sub>2</sub>

Two types of malonate decarboxylase are currently known, both of which form multienzyme complexes.

== References ==
{{reflist}}

== External links ==
* {{MeshName|Biotin-independent+malonate+decarboxylase}}



[[Category:EC 4.1.1]]