:Biotin-independent malonate decarboxylase

{{Infobox enzyme

| Name = Biotin-independent malonate decarboxylase

| EC_number = 4.1.1.88

| CAS_number =

| GO_code =

| image =

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Biotin-independent malonate decarboxylase ({{EnzExplorer|4.1.1.88}}, malonate decarboxylase (without biotin), malonate decarboxylase, MDC) is an enzyme with systematic name malonate carboxy-lyase (biotin-independent).{{cite journal | vauthors = Schmid M, Berg M, Hilbi H, Dimroth P | title = Malonate decarboxylase of Klebsiella pneumoniae catalyses the turnover of acetyl and malonyl thioester residues on a coenzyme-A-like prosthetic group | journal = European Journal of Biochemistry | volume = 237 | issue = 1 | pages = 221–8 | date = April 1996 | pmid = 8620876 | doi = 10.1111/j.1432-1033.1996.0221n.x }}{{cite journal | title = Subunit organization of bacterial malonate decarboxylases: the smallest δ subunit as an acyl-carrier protein |author1 = Byun, H.S. |author2 =Kim, Y.S. |journal = J. Biochem. Mol. Biol. |year = 1997 |volume = 30 |pages = 132–137 }}{{cite journal | vauthors = Hoenke S, Schmid M, Dimroth P | title = Sequence of a gene cluster from Klebsiella pneumoniae encoding malonate decarboxylase and expression of the enzyme in Escherichia coli | journal = European Journal of Biochemistry | volume = 246 | issue = 2 | pages = 530–8 | date = June 1997 | pmid = 9208947 | doi = 10.1111/j.1432-1033.1997.00530.x | doi-access = free }}{{cite journal | vauthors = Chohnan S, Fujio T, Takaki T, Yonekura M, Nishihara H, Takamura Y | title = Malonate decarboxylase of Pseudomonas putida is composed of five subunits | journal = FEMS Microbiology Letters | volume = 169 | issue = 1 | pages = 37–43 | date = December 1998 | pmid = 9851033 | doi = 10.1111/j.1574-6968.1998.tb13296.x | doi-access = free }}{{cite journal | vauthors = Hoenke S, Schmid M, Dimroth P | title = Identification of the active site of phosphoribosyl-dephospho-coenzyme A transferase and relationship of the enzyme to an ancient class of nucleotidyltransferases | journal = Biochemistry | volume = 39 | issue = 43 | pages = 13233–40 | date = October 2000 | pmid = 11052676 | doi = 10.1021/bi001154u }}{{cite journal | vauthors = Handa S, Koo JH, Kim YS, Floss HG | title = Stereochemical course of biotin-independent malonate decarboxylase catalysis | journal = Archives of Biochemistry and Biophysics | volume = 370 | issue = 1 | pages = 93–6 | date = October 1999 | pmid = 10496981 | doi = 10.1006/abbi.1999.1369 }}{{cite journal | vauthors = Koo JH, Kim YS | title = Functional evaluation of the genes involved in malonate decarboxylation by Acinetobacter calcoaceticus | journal = European Journal of Biochemistry | volume = 266 | issue = 2 | pages = 683–90 | date = December 1999 | pmid = 10561613 | doi = 10.1046/j.1432-1327.1999.00924.x | doi-access = free }}{{cite journal | vauthors = Kim YS | title = Malonate metabolism: biochemistry, molecular biology, physiology, and industrial application | journal = Journal of Biochemistry and Molecular Biology | volume = 35 | issue = 5 | pages = 443–51 | date = September 2002 | pmid = 12359084 | doi = 10.5483/bmbrep.2002.35.5.443 | doi-access = free }}{{cite journal | vauthors = Dimroth P, Hilbi H | title = Enzymic and genetic basis for bacterial growth on malonate | journal = Molecular Microbiology | volume = 25 | issue = 1 | pages = 3–10 | date = July 1997 | pmid = 11902724 | doi = 10.1046/j.1365-2958.1997.4611824.x | doi-access = free }} This enzyme catalyses the following chemical reaction

: malonate + H⁺ $\backslash rightleftharpoons$ acetate + CO₂

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