Information on EC 4.1.1.87 - malonyl-S-ACP decarboxylase

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The enzyme appears in viruses and cellular organisms

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
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].
CAS REGISTRY NUMBER
COMMENTARY hide
80700-20-5
multienzyme complex malonate decarboxylase
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
beta subunit of malonate decarboxylase complex
UniProt
Manually annotated by BRENDA team
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
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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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.19
isolated beta subunit of malonate decarboxylase complex
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
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
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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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