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Literature summary for 4.1.1.9 extracted from

  • Aparicio, D.; Perez-Luque, R.; Carpena, X.; Diaz, M.; Ferrer, J.C.; Loewen, P.C.; Fita, I.
    Structural asymmetry and disulfide bridges among subunits modulate the activity of human malonyl-CoA decarboxylase (2013), J. Biol. Chem., 288, 11907-11919.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.1.1.9

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes as maltose-binding protein fusion proteins in Escherichia coli strain BL21(DE3) in minimal medium containing selenomethionine Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant detagged enzyme, from 15% PEG 2000 monomethyl ether and 0.1 M sodium acetate, pH 4.5, and 10 mM sodium citrate, sitting drop vapor diffusion method, X-ray diffraction structure determination and analysis at 3.3-4.3 A resolution, molecular replacement Homo sapiens

Protein Variants

Protein Variants Comment Organism
C206S site-directed mutagenesis Homo sapiens
C206S/C243S site-directed mutagenesis Homo sapiens
C243S site-directed mutagenesis Homo sapiens
E302G site-directed mutagenesis Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten steady-state kinetics, overview Homo sapiens
0.22
-
 malonyl-CoA pH 8.5, temperature not specified in the publication, mutant E302G, no H2O2 Homo sapiens
0.35
-
 malonyl-CoA pH 8.5, temperature not specified in the publication, wild-type enzyme, 0.2 M H2O2 Homo sapiens
0.42
-
 malonyl-CoA pH 8.5, temperature not specified in the publication, wild-type enzyme, 0.1 M H2O2 Homo sapiens
0.46
-
 malonyl-CoA pH 8.5, temperature not specified in the publication, wild-type enzyme, 0.05 M H2O2 Homo sapiens
0.56
-
 malonyl-CoA pH 8.5, temperature not specified in the publication, mutant C243S, 0.2 M H2O2 Homo sapiens
0.58
-
 malonyl-CoA pH 8.5, temperature not specified in the publication, mutant C243S, no H2O2 Homo sapiens
0.68
-
 malonyl-CoA pH 8.5, temperature not specified in the publication, mutant C243S, 0.1 M H2O2 Homo sapiens
0.73
-
 malonyl-CoA pH 8.5, temperature not specified in the publication, mutant C206S, no H2O2 Homo sapiens
0.79
-
 malonyl-CoA pH 8.5, temperature not specified in the publication, mutant C206S, 0.2 M H2O2 Homo sapiens
0.8 1 malonyl-CoA pH 8.5, temperature not specified in the publication, mutant C206S/C243S, 0.2 M H2O2 Homo sapiens
0.83
-
 malonyl-CoA pH 8.5, temperature not specified in the publication, wild-type enzyme, no H2O2 Homo sapiens
0.99
-
 malonyl-CoA pH 8.5, temperature not specified in the publication, mutant C206S/C243S, 0.1 M H2O2 Homo sapiens
1.04
-
 malonyl-CoA pH 8.5, temperature not specified in the publication, mutant C206S, 00.1 M H2O2 Homo sapiens
1.16
-
 malonyl-CoA pH 8.5, temperature not specified in the publication, mutant C206S/C243S, no H2O2 Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
additional information multiple intracellular locations of the enzyme Homo sapiens
-
-
peroxisome
-
 Homo sapiens 5777
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Malonyl-CoA Homo sapiens
-
 Acetyl-CoA + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens O95822
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant maltose-binding protein fusion wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by amylase affinity chromatography, fusion protein cleavage by tobacco etch virus protease, gel filtration, and anion exchange chromatography Homo sapiens

Reaction

Reaction Comment Organism Reaction ID
malonyl-CoA = acetyl-CoA + CO2 half-of-the-sites reaction mechanism, overview Homo sapiens
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Malonyl-CoA
-
 Homo sapiens Acetyl-CoA + CO2
-
 ?
additional information docking analysis of the enzyme onto peroxin 5. modeling, overview Homo sapiens ?
-
 ?

Subunits

Subunits Comment Organism
More structure analysis, overview. Structural asymmetry and disulfide bridges among subunits modulate the activity of the enzyme. Intersubunit disulfide bridges, Cys206-Cys206 and Cys243-Cys243, can link the four subunits of the tetramer, imparting positive cooperativity to the catalytic process Homo sapiens
tetramer a dimer of structural heterodimers, in which the two subunits present markedly different conformations. Each subunit has an all-helix N-terminal domain and a catalytic C-terminal domain with an acetyltransferase fold. The N-terminal domain of each monomer, Met40-Trp189, contains eight alpha-helices organized as a bundle of four antiparallel helices (alpha1-alpha3 and alpha6) with two pairs of helices inserted (alpha4-alpha5 and alpha7-alpha8), a four-helix bundle variant. H2O2 oxidation is apparently cooperative in the sense that linked tetramers are formed preferentially to dimers Homo sapiens

Synonyms

Synonyms Comment Organism
MCD
-
 Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
13.3
-
 malonyl-CoA pH 8.5, temperature not specified in the publication, mutant E302G, no H2O2 Homo sapiens
94.6
-
 malonyl-CoA pH 8.5, temperature not specified in the publication, mutant C243S, no H2O2 Homo sapiens
109.2
-
 malonyl-CoA pH 8.5, temperature not specified in the publication, wild-type enzyme, 0.2 M H2O2 Homo sapiens
114.2
-
 malonyl-CoA pH 8.5, temperature not specified in the publication, mutant C206S, 0.2 M H2O2 Homo sapiens
117.1
-
 malonyl-CoA pH 8.5, temperature not specified in the publication, mutant C206S, no H2O2 Homo sapiens
128.3
-
 malonyl-CoA pH 8.5, temperature not specified in the publication, wild-type enzyme, 0.05 M H2O2 Homo sapiens
135
-
 malonyl-CoA pH 8.5, temperature not specified in the publication, wild-type enzyme, 0.1 M H2O2 Homo sapiens
137.5
-
 malonyl-CoA pH 8.5, temperature not specified in the publication, mutant C243S, 0.1 M H2O2 Homo sapiens
141.2
-
 malonyl-CoA pH 8.5, temperature not specified in the publication, mutant C206S, 00.1 M H2O2 Homo sapiens
141.2
-
 malonyl-CoA pH 8.5, temperature not specified in the publication, wild-type enzyme, no H2O2 Homo sapiens
162.5
-
 malonyl-CoA pH 8.5, temperature not specified in the publication, mutant C206S/C243S, no H2O2 Homo sapiens
167.1
-
 malonyl-CoA pH 8.5, temperature not specified in the publication, mutant C206S/C243S, 0.2 M H2O2 Homo sapiens
175.4
-
 malonyl-CoA pH 8.5, temperature not specified in the publication, mutant C206S/C243S, 0.1 M H2O2 Homo sapiens
208.3
-
 malonyl-CoA pH 8.5, temperature not specified in the publication, mutant C243S, 0.2 M H2O2 Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
 assay at Homo sapiens

General Information

General Information Comment Organism
additional information structural asymmetry and disulfide bridges among subunits modulate the activity of the enzyme. The molecular organization of dimer of structural heterodimers, in which the two subunits present markedly different conformations, is consistent with half-of-the-sites reactivity. Interactions extend beyond the C-terminal targeting motif. Active site structure, overview Homo sapiens
physiological function decarboxylation of malonyl-CoA to acetyl-CoA by malonyl-CoA decarboxylase is an essential facet in the regulation of fatty acid metabolism Homo sapiens

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.00006
-
 malonyl-CoA pH 8.5, temperature not specified in the publication, mutant E302G, no H2O2 Homo sapiens
0.00014
-
 malonyl-CoA pH 8.5, temperature not specified in the publication, mutant C206S, 00.1 M H2O2 Homo sapiens
0.00014
-
 malonyl-CoA pH 8.5, temperature not specified in the publication, mutant C206S/C243S, no H2O2 Homo sapiens
0.00015
-
 malonyl-CoA pH 8.5, temperature not specified in the publication, mutant C206S, 0.2 M H2O2 Homo sapiens
0.00016
-
 malonyl-CoA pH 8.5, temperature not specified in the publication, mutant C206S, no H2O2 Homo sapiens
0.00016
-
 malonyl-CoA pH 8.5, temperature not specified in the publication, mutant C243S, no H2O2 Homo sapiens
0.00017
-
 malonyl-CoA pH 8.5, temperature not specified in the publication, wild-type enzyme, no H2O2 Homo sapiens
0.00018
-
 malonyl-CoA pH 8.5, temperature not specified in the publication, mutant C206S/C243S, 0.1 M H2O2 Homo sapiens
0.0002
-
 malonyl-CoA pH 8.5, temperature not specified in the publication, mutant C206S/C243S, 0.2 M H2O2 Homo sapiens
0.0002
-
 malonyl-CoA pH 8.5, temperature not specified in the publication, mutant C243S, 0.1 M H2O2 Homo sapiens
0.00028
-
 malonyl-CoA pH 8.5, temperature not specified in the publication, wild-type enzyme, 0.05 M H2O2 Homo sapiens
0.00031
-
 malonyl-CoA pH 8.5, temperature not specified in the publication, wild-type enzyme, 0.2 M H2O2 Homo sapiens
0.00032
-
 malonyl-CoA pH 8.5, temperature not specified in the publication, wild-type enzyme, 0.1 M H2O2 Homo sapiens
0.00037
-
 malonyl-CoA pH 8.5, temperature not specified in the publication, mutant C243S, 0.2 M H2O2 Homo sapiens