Information on EC 4.1.1.87 - malonyl-S-ACP decarboxylase

for references in articles please use BRENDA:EC4.1.1.87
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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
4.1.1.87
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RECOMMENDED NAME
GeneOntology No.
malonyl-S-ACP decarboxylase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a malonyl-[acyl-carrier protein] + H+ = an acetyl-[acyl-carrier protein] + CO2
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
malonate degradation I (biotin-independent)
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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].
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CAS REGISTRY NUMBER
COMMENTARY hide
80700-20-5
multienzyme complex malonate decarboxylase
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
beta subunit of malonate decarboxylase complex
UniProt
Manually annotated by BRENDA team
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
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LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
malonyl-CoA + H+
acetyl-CoA + CO2
show the reaction diagram
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?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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the binding site for the acyl residues on the acyl carrier protein is 2'-(5''-phosphoribosyl)-3'-dephospho-CoA
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithioerythritol
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formation of a catalytically inactive SH-enzyme from the catalytically active acetyl-S-enzyme
hydroxylamine
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formation of a catalytically inactive SH-enzyme from the catalytically active acetyl-S-enzyme
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.19
isolated beta subunit of malonate decarboxylase complex
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
12000
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1 * 65000, alpha subunit, 1* 34000, beta-subunit, 1 * 30000, gamma subunit, 1 * 12000, delta subunit, SDS-PAGE
30000
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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
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1 * 65000, alpha subunit, 1* 34000, beta-subunit, 1 * 30000, gamma subunit, 1 * 12000, delta subunit, SDS-PAGE
142000
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gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 33000, SDS-PAGE, isolated beta subunit of malonate decarboxylase complex
tetramer
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1 * 65000, alpha subunit, 1* 34000, beta-subunit, 1 * 30000, gamma subunit, 1 * 12000, delta subunit, SDS-PAGE
additional information
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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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
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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)