EC 4.1.1.87 - Malonyl-S-ACP decarboxylase

  IntEnz view ENZYME view
XML

IntEnz Enzyme Nomenclature
EC 4.1.1.87

Names

Accepted name:
malonyl-S-ACP decarboxylase
Other names:
malonyl-S-acyl-carrier protein decarboxylase
MdcD/MdcE
MdcD,E
Systematic name:
malonyl-[acyl-carrier-protein] carboxy-lyase

Reaction

Comments:

This enzyme comprises the β and γ subunits of EC 4.1.1.88 (biotin-independent malonate decarboxylase) but is not present in EC 4.1.1.89 (biotin-dependent malonate decarboxylase). It follows on from EC 2.3.1.187, acetyl-S-ACP:malonate ACP transferase, and results in the regeneration of the acetylated form of the acyl-carrier-protein subunit of malonate decarboxylase [5]. The carboxy group is lost with retention of configuration [3].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot:

References

  1. Schmid, M., Berg, M., Hilbi, H. and Dimroth, P.
    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 (1996). [PMID: 8620876]
  2. Koo, J.H. and Kim, Y.S.
    Functional evaluation of the genes involved in malonate decarboxylation by Acinetobacter calcoaceticus.
    Eur. J. Biochem. 266 : 683-690 (1999). [PMID: 10561613]
  3. Handa, S., Koo, J.H., Kim, Y.S. and Floss, H.G.
    Stereochemical course of biotin-independent malonate decarboxylase catalysis.
    Arch. Biochem. Biophys. 370 : 93-96 (1999). [PMID: 10496981]
  4. Chohnan, S., Akagi, K. and Takamura, Y.
    Functions of malonate decarboxylase subunits from Pseudomonas putida.
    Biosci. Biotechnol. Biochem. 67 : 214-217 (2003). [PMID: 12619701]
  5. Dimroth, P. and Hilbi, H.
    Enzymic and genetic basis for bacterial growth on malonate.
    Mol. Microbiol. 25 : 3-10 (1997). [PMID: 11902724]

[EC 4.1.1.87 created 2008]