Enzyme

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     4. Lyases
        4.1 Carbon-carbon lyases
            4.1.1 Carboxy-lyases
ID:4.1.1.87
Description:Malonyl-S-ACP decarboxylase.
Alternative Name: Malonyl-S-acyl-carrier protein decarboxylase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 4.1.1.87
BRENDA Enzyme Link: BRENDA 4.1.1.87
KEGG Enzyme Link: KEGG4.1.1.87
BioCyc Enzyme Link: BioCyc 4.1.1.87
ExPASy Enzyme Link: ExPASy4.1.1.87
EC2PDB Enzyme Link: EC2PDB 4.1.1.87
ExplorEnz Enzyme Link: ExplorEnz 4.1.1.87
PRIAM enzyme-specific profiles Link: PRIAM 4.1.1.87
IntEnz Enzyme Link: IntEnz 4.1.1.87
MEDLINE Enzyme Link: MEDLINE 4.1.1.87
MSA:

4.1.1.87;

Phylogenetic Tree:

4.1.1.87;

Uniprot:
M-CSA:
RHEA:24460 H(+) + malonyl-[ACP] = acetyl-[ACP] + CO2
RULE(radius=1) [C:1][C:2](=[O:3])[OH:4]>>[C:1].[O:3]=[C:2]=[O:4]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Malonate decarboxylase of Klebsiella pneumoniae catalyses the turnover of acetyl and malonyl thioester residues on a coenzyme-A-like prosthetic group.Schmid M, Berg M, Hilbi H, Dimroth P1996 Apr 18620876
Convergence of isoprene and polyketide biosynthetic machinery: isoprenyl-S-carrier proteins in the pksX pathway of Bacillus subtilis.Calderone CT, Kowtoniuk WE, Kelleher NL, Walsh CT, Dorrestein PC2006 Jun 1316757561
Stereochemical course of biotin-independent malonate decarboxylase catalysis.Handa S, Koo JH, Kim YS, Floss HG1999 Oct 110496981