EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
2.3.1.39 | dithiothreitol | stimulates | Escherichia coli | |
2.3.1.41 | 2-mercaptoethanol | activation | Escherichia coli | |
2.3.1.41 | phosphate | activation, 0.2 M | Escherichia coli |
EC Number | Application | Comment | Organism |
---|---|---|---|
2.7.8.7 | analysis | enzyme can be utilized in an assay for apo-ACP in biological material | Escherichia coli |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
2.3.1.41 | - |
Escherichia coli |
EC Number | General Stability | Organism |
---|---|---|
2.7.8.7 | very unstable, markedly protected from inactivation by the presence of half-saturating concentrations of reduced CoA | Escherichia coli |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.3.1.38 | iodoacetamide | acetyl-CoA protects | Escherichia coli | |
2.3.1.38 | N-ethylmaleimide | acetyl-CoA protects | Escherichia coli | |
2.3.1.39 | additional information | no inhibition by sulfhydryl inhibitors | Escherichia coli | |
2.3.1.39 | p-chloromercuribenzoate | strong | Escherichia coli | |
2.3.1.39 | phenylmethanesulfonyl fluoride | - |
Escherichia coli | |
2.3.1.41 | iodoacetamide | - |
Escherichia coli | |
2.3.1.41 | N-ethylmaleimide | - |
Escherichia coli |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.3.1.41 | additional information | - |
additional information | - |
Escherichia coli | |
2.7.8.7 | 0.0004 | - |
apo-acyl-carrier protein | - |
Escherichia coli | |
2.7.8.7 | 0.15 | - |
CoA | pH 8.0, 33°C | Escherichia coli |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
2.3.1.41 | cytosol | - |
Escherichia coli | 5829 | - |
2.7.8.7 | cytoplasm | - |
Escherichia coli | 5737 | - |
2.7.8.7 | cytoplasm | - |
Saccharomyces cerevisiae | 5737 | - |
2.7.8.7 | cytoplasm | - |
Clostridium kluyveri | 5737 | - |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
2.7.8.7 | Mg2+ | maximal activity at 0.025 mM | Escherichia coli | |
2.7.8.7 | additional information | CuSO4, CdCl2 and CrCl2 does not stimulate the reaction at any ceoncentration, trivalent metal cations such as FeCl3 or AlCl3 are ineffective | Escherichia coli |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
2.3.1.41 | 34000 | - |
2 * 34000, SDS-PAGE | Escherichia coli |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.3.1.39 | malonyl-CoA + acyl-carrier protein | Escherichia coli | initial reaction in de novo fatty acid synthesis, part of non-associated fatty acid synthase system of plants and prokaryotes | CoA + malonyl-acyl-carrier protein | - |
? | |
2.7.8.7 | CoA + apo-[acyl-carrier protein] | Escherichia coli | - |
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein] | - |
r | |
2.7.8.7 | CoA + apo-[acyl-carrier protein] | Saccharomyces cerevisiae | - |
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein] | - |
r |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.3.1.38 | Escherichia coli | - |
- |
- |
2.3.1.39 | Escherichia coli | - |
- |
- |
2.3.1.41 | Escherichia coli | - |
- |
- |
2.7.8.7 | Clostridium kluyveri | - |
- |
- |
2.7.8.7 | Escherichia coli | - |
- |
- |
2.7.8.7 | Rattus norvegicus | - |
rat | - |
2.7.8.7 | Saccharomyces cerevisiae | - |
yeast | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.3.1.39 | DEAE-cellulose and DEAE-Sephadex chromatography | Escherichia coli |
2.3.1.41 | - |
Escherichia coli |
2.7.8.7 | partially | Escherichia coli |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
2.3.1.39 | malonyl-CoA + an [acyl-carrier protein] = CoA + a malonyl-[acyl-carrier protein] | mechanism, formation of a malonyl-enzyme intermediate | Escherichia coli | |
2.3.1.41 | an acyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein] = a 3-oxoacyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein] | mechanism | Escherichia coli |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
2.7.8.7 | liver | - |
Rattus norvegicus | - |
EC Number | Storage Stability | Organism |
---|---|---|
2.3.1.41 | -20°C, 90% loss of activity within 1 year | Escherichia coli |
2.3.1.41 | -20°C, at least 1 month | Escherichia coli |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.3.1.38 | acetyl-CoA + [acyl-carrier protein] | acetyl-S-pantetheine can replace acetyl-CoA | Escherichia coli | CoA + acetyl-[acyl-carrier protein] | - |
? | |
2.3.1.38 | butyryl-CoA + [acyl-carrier protein] | - |
Escherichia coli | CoA + butyryl-[acyl-carrier protein] | - |
? | |
2.3.1.38 | hexanoyl-CoA + [acyl-carrier protein] | - |
Escherichia coli | CoA + hexanoyl-[acyl-carrier protein] | - |
? | |
2.3.1.38 | additional information | in vertebrates, yeast and Mycobacteria acetyl transferase activity is a domain of the multifunctional polypeptide chains of fatty acid synthase EC 2.3.1.85 and EC 2.3.1.86 | Escherichia coli | ? | - |
? | |
2.3.1.38 | octanoyl-CoA + [acyl-carrier protein] | - |
Escherichia coli | CoA + octanoyl-[acyl-carrier protein] | - |
? | |
2.3.1.39 | malonyl-CoA + acyl-carrier protein | acetyl-CoA cannot replace malonyl-CoA | Escherichia coli | CoA + malonyl-[acyl-carrier protein] | - |
? | |
2.3.1.39 | malonyl-CoA + acyl-carrier protein | characterization of acyl-carrier protein | Escherichia coli | CoA + malonyl-[acyl-carrier protein] | - |
? | |
2.3.1.39 | malonyl-CoA + acyl-carrier protein | via stable covalent malonyl-enzyme intermediate | Escherichia coli | CoA + malonyl-[acyl-carrier protein] | - |
? | |
2.3.1.39 | malonyl-CoA + acyl-carrier protein | initial reaction in de novo fatty acid synthesis, part of non-associated fatty acid synthase system of plants and prokaryotes | Escherichia coli | CoA + malonyl-acyl-carrier protein | - |
? | |
2.3.1.39 | malonyl-CoA + pantetheine | - |
Escherichia coli | malonyl-pantetheine + CoA | - |
? | |
2.3.1.39 | malonyl-pantetheine + acyl-carrier protein | - |
Escherichia coli | pantetheine + malonyl-[acyl-carrier protein] | - |
? | |
2.3.1.41 | acetyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] | - |
Escherichia coli | acetoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein] | - |
? | |
2.3.1.41 | cis-mono-unsaturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] | - |
Escherichia coli | cis-mono-unsaturated 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein] | - |
? | |
2.3.1.41 | saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] | not hexadecanoyl-[acyl-carrier-protein] | Escherichia coli | 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein] | - |
? | |
2.3.1.41 | saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] | specific for acyl-[acyl-carrier-protein] thioesters, not acyl-CoA or acyl pantetheine thioesters | Escherichia coli | 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein] | - |
? | |
2.7.8.7 | CoA + apo-[acyl-carrier protein] | - |
Escherichia coli | adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein] | - |
r | |
2.7.8.7 | CoA + apo-[acyl-carrier protein] | - |
Saccharomyces cerevisiae | adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein] | - |
r | |
2.7.8.7 | additional information | specificity of the holo-ACP synthetase is not examined in detail, only CoA is the donor of the 4'-phosphopantetheine moiety, dephospho-CoA is essentially inactive | Escherichia coli | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.3.1.38 | More | vertebrates, yeast and Mycobacteria fatty acid synthetases contain all individual activities on one or two multifunctional polypeptide chains, plant, Escherichia coli and other prokaryotic fatty acid synthases are non-associated systems of individual enzymes | Escherichia coli |
2.3.1.41 | dimer | 2 * 34000, SDS-PAGE | Escherichia coli |
2.3.1.41 | More | vertebrates, yeast and Mycobacteria fatty acid synthetases contain all individual activities on one or two multifunctional polypeptide chains, plant, Escherichia coli and other prokaryotic fatty acid synthases are non-associated systems of individual enzymes | Escherichia coli |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.3.1.41 | More | in vertebrates, yeast and Mycobacteria beta-ketoacyl synthase activity is a domain of the multifunctional polypeptide chains of fatty acid synthase EC 2.3.1.85 and EC 2.3.1.86 | Escherichia coli |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.3.1.41 | 30 | - |
assay at | Escherichia coli |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.3.1.41 | 100 | - |
inactivation after 1 min | Escherichia coli |