Information on EC 2.1.3.10 - malonyl-S-ACP:biotin-protein carboxyltransferase

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The expected taxonomic range for this enzyme is: Malonomonas rubra

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EC NUMBER
COMMENTARY hide
2.1.3.10
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RECOMMENDED NAME
GeneOntology No.
malonyl-S-ACP:biotin-protein carboxyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a malonyl-[acyl-carrier protein] + a biotinyl-[protein] = an acetyl-[acyl-carrier protein] + a carboxybiotinyl-[protein]
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
malonate degradation II (biotin-dependent)
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SYSTEMATIC NAME
IUBMB Comments
malonyl-[acyl-carrier protein]:biotinyl-[protein] carboxytransferase
Derived from the components MadC and MadD of the anaerobic bacterium Malonomonas rubra, this enzyme is a component of EC 4.1.1.89, biotin-dependent malonate decarboxylase. The carboxy group is transferred from malonate to the prosthetic group of the biotin protein (MadF) with retention of configuration [2]. Similar to EC 4.1.1.87, malonyl-S-ACP decarboxylase, which forms part of the biotin-independent malonate decarboxylase (EC 4.1.1.88), this enzyme also follows on from EC 2.3.1.187, acetyl-S-ACP:malonate ACP transferase, and results in the regeneration of the acetyl-[acyl-carrier protein] [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
enzyme is part of the Na+-activied malonate decarboxylase system
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Manually annotated by BRENDA team
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + dephospho-CoA
CoA + acetyl-dephospho-CoA
show the reaction diagram
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r
malonyl-CoA + dephospho-CoA
CoA + malonyl-dephospho-CoA
show the reaction diagram
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r
additional information
?
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enzyme catalyzes the transfer of acyl carrier protein from acetyl acyl carrier protein and malonate to yield malonyl acyl carrier protein and acetate. Malonate is thus activated on the enzyme by exchange for the catalytically important enzyme-bound acetyl thioester residues
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + dephospho-CoA
CoA + acetyl-dephospho-CoA
show the reaction diagram
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-
-
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r
malonyl-CoA + dephospho-CoA
CoA + malonyl-dephospho-CoA
show the reaction diagram
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r
additional information
?
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enzyme catalyzes the transfer of acyl carrier protein from acetyl acyl carrier protein and malonate to yield malonyl acyl carrier protein and acetate. Malonate is thus activated on the enzyme by exchange for the catalytically important enzyme-bound acetyl thioester residues
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
malonate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
54
acetate
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pH 6.0
6.9
acetyl-CoA
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pH 6.0
0.5
malonate
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pH 6.0
1.9
malonyl-CoA
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pH 6.0
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3
citrate
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pH 6.0
0.4
malonate
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pH 6.0
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5
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sharp decrease in activity from pH 5.5 to pH 4.5
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
59000
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gel filtration
67000
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1 * 67000, SDS-PAGE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 67000, SDS-PAGE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purification of subunit acetyl-S-acyl carrier protein: malonate acyl carrier protein-SH transferase
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LINKS TO OTHER DATABASES (specific for EC-Number 2.1.3.10)
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)