Information on EC 4.1.1.87 - malonyl-S-ACP decarboxylase

for references in articles please use BRENDA:EC4.1.1.87
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:

The enzyme appears in viruses and cellular organisms

top print hide
EC NUMBER
COMMENTARY hide
4.1.1.87
-
top print hide
RECOMMENDED NAME
GeneOntology No.
malonyl-S-ACP decarboxylase
-
top print hide
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a malonyl-[acyl-carrier protein] + H+ = an acetyl-[acyl-carrier protein] + CO2
show the reaction diagram
top print hide
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
malonate degradation I (biotin-independent)
-
-
top print hide
SYSTEMATIC NAME
IUBMB Comments
malonyl-[acyl-carrier-protein] carboxy-lyase
This enzyme comprises the beta and gamma 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].
top
top print hide
CAS REGISTRY NUMBER
COMMENTARY hide
80700-20-5
multienzyme complex malonate decarboxylase
top print hide
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
beta subunit of malonate decarboxylase complex
UniProt
Manually annotated by BRENDA team
top print hide
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
malonyl-CoA + H+
acetyl-CoA + CO2
show the reaction diagram
-
-
-
?
top print hide
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
the binding site for the acyl residues on the acyl carrier protein is 2'-(5''-phosphoribosyl)-3'-dephospho-CoA
-
top print hide
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithioerythritol
-
formation of a catalytically inactive SH-enzyme from the catalytically active acetyl-S-enzyme
hydroxylamine
-
formation of a catalytically inactive SH-enzyme from the catalytically active acetyl-S-enzyme
top print hide
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
top print hide
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.19
isolated beta subunit of malonate decarboxylase complex
top print hide
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
12000
-
1 * 65000, alpha subunit, 1* 34000, beta-subunit, 1 * 30000, gamma subunit, 1 * 12000, delta subunit, SDS-PAGE
30000
-
1 * 65000, alpha subunit, 1* 34000, beta-subunit, 1 * 30000, gamma subunit, 1 * 12000, delta subunit, SDS-PAGE
33000
2 * 33000, SDS-PAGE, isolated beta subunit of malonate decarboxylase complex
65000
-
1 * 65000, alpha subunit, 1* 34000, beta-subunit, 1 * 30000, gamma subunit, 1 * 12000, delta subunit, SDS-PAGE
142000
-
gel filtration
top print hide
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 33000, SDS-PAGE, isolated beta subunit of malonate decarboxylase complex
tetramer
-
1 * 65000, alpha subunit, 1* 34000, beta-subunit, 1 * 30000, gamma subunit, 1 * 12000, delta subunit, SDS-PAGE
additional information
top print hide
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
top print hide
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
top print hide
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
reacylation of the catalytically inactive SH-enzyme to form the catalytically active acetyl-S-enzyme can be achieved with acetic anhydride or more efficiently with malonyl-CoA
-
top
top
top
LINKS TO OTHER DATABASES (specific for EC-Number 4.1.1.87)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)