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 (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 | 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 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 | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
additional information | multiple intracellular locations of the enzyme | Homo sapiens | - |
- |
peroxisome | - |
Homo sapiens | 5777 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
Malonyl-CoA | Homo sapiens | - |
Acetyl-CoA + CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | O95822 | - |
- |
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 | Comment | Organism | Reaction ID |
---|---|---|---|
malonyl-CoA = acetyl-CoA + CO2 | half-of-the-sites reaction mechanism, overview | Homo sapiens |
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 | 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 | Comment | Organism |
---|---|---|
MCD | - |
Homo sapiens |
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 Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8.5 | - |
assay at | Homo sapiens |
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 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 |