Information on EC 4.1.1.88 - biotin-independent malonate decarboxylase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
4.1.1.88
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RECOMMENDED NAME
GeneOntology No.
biotin-independent malonate decarboxylase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
malonate + H+ = acetate + CO2
show the reaction diagram
SYSTEMATIC NAME
IUBMB Comments
malonate carboxy-lyase (biotin-independent)
Two types of malonate decarboxylase are currently known, both of which form multienzyme complexes. This enzyme is a cytosolic protein that is biotin-independent. The other type is a biotin-dependent, Na+-translocating enzyme that includes both soluble and membrane-bound components (cf. EC 4.1.1.89, biotin-dependent malonate decarboxylase). As free malonate is chemically rather inert, it has to be activated prior to decarboxylation. In both enzymes, this is achieved by exchanging malonate with an acetyl group bound to an acyl-carrier protiein (ACP), to form malonyl-ACP and acetate, with subsequent decarboxylation regenerating the acetyl-ACP. The ACP subunit of both enzymes differs from that found in fatty-acid biosynthesis by having phosphopantethine attached to a serine side-chain as 2-(5-triphosphoribosyl)-3-dephospho-CoA rather than as phosphopantetheine 4'-phosphate. The individual enzymes involved in carrying out the reaction of this enzyme complex are EC 2.3.1.187 (acetyl-S-ACP:malonate ACP transferase), EC 2.3.1.39 ([acyl-carrier-protein] S-malonyltransferase) and EC 4.1.1.87 (malonyl-S-ACP decarboxylase). The carboxy group is lost with retention of configuration [6].
CAS REGISTRY NUMBER
COMMENTARY hide
80700-20-5
multienzyme complex malonate decarboxylase
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-ethylmalonate + H+
butanoate + CO2
show the reaction diagram
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0.8% of the activity with malonate
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-
?
2-methylmalonate + H+
propionate + CO2
show the reaction diagram
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24% of the activity with malonate
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?
glutarate + H+
butanoate + CO2
show the reaction diagram
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1.1% of the activity with malonate
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-
?
malonate + H+
acetate + CO2
show the reaction diagram
oxalate + H+
CO2
show the reaction diagram
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1.1% of the activity with malonate
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-Nitro-5-thiocyanobenzoic acid
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0.64 mM, 2.1% residual activity
5,5'-dithio-bis(2-nitrobenzoic acid)
Bromoacetate
diethyldicarbonate
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
iodoacetamide
N-Acetylimidazole
N-ethylmaleimide
pyridoxal 5'phosphate
Sodium borohydride
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inactivation
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
diethyldicarbonate
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1 mM, 114% of initial activity
N-Acetylimidazole
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1 mM, 117% of initial activity
pyridoxal 5'phosphate
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1 mM, 112% of initial activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.11 - 3.23
malonate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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the alpha subunit shows CoA-transferase activity with specific activity of 39.03 U/mg
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.4
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isoelectric focusing
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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
33000
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2 * 65000, alpha subunit, 1 * 33000, beta subunit, 1 * 30000, gamma subunit, 1 * 11000, delta subunit
142000
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gel filtration
185000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
multimer
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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme is sensitive to repeated freezing and thawing
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, stable for several months
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4C, deacetylated enzyme, full reactivation by addition of malonyl-CoA during 2 months storage
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression of gene cluster in Escherichia coli, no enzymatic activity
O54414 and O54416 and O54417 and O54415
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
O54414 and O54416 and O54417 and O54415
expression of gene cluster containing subunits alpha, beta, gamma, delta in Escherichia coli, no enzymatic activity
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
reactivation of deacetyl malonate decarboxylase with malonyl-CoA, acetyl-CoA or methylmalonyl-CoA to more than 80% of initial activity
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reactivation of deacetyl malonate decarboxylase with malonyl-CoA, acetyl-CoA or methylmalonyl-CoA to more than 80% of initial activity; reactivation of deacetyl malonate decarboxylase with malonyl-CoA to 100%, with acetyl-CoA or methylmalonyl-CoA to about 50% of initial activity, respectively
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reactivation of deacetylated enzyme by incubation with acetic anhydride or malonyl-CoA
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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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