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Literature summary extracted from

  • Vagelos, R.P.
    Acyl group transfer (acyl carrier protein) (1973), The Enzymes, 3rd Ed. (Boyer, P. D. , ed. ), 8, 155-199.
No PubMed abstract available

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.3.1.41 2-mercaptoethanol activation Escherichia coli
2.3.1.41 dithiothreitol activation Escherichia coli
2.3.1.41 EDTA activation Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.1.41
-
 Escherichia coli

General Stability

EC Number General Stability Organism
2.3.1.39 salt concentrations above 0.1 M inactivate Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.1.39 acetyl-CoA competitive to malonyl-CoA Escherichia coli
2.3.1.39 iodoacetamide malonyl-CoA protects; pH-dependent Escherichia coli
2.3.1.39 iodoacetate
-
 Escherichia coli
2.3.1.39 additional information
-
 Escherichia coli
2.3.1.39 p-chloromercuribenzoate pH-independent Escherichia coli
2.3.1.39 phenylmethanesulfonyl fluoride malonyl-CoA protects Escherichia coli
2.3.1.41 iodoacetamide no inhibition of malonyl-[acyl-carrier-protein]-decarboxylation Escherichia coli
2.3.1.41 N-ethylmaleimide no inhibition of malonyl-[acyl-carrier-protein]-decarboxylation Clostridium kluyveri
2.3.1.41 N-ethylmaleimide no inhibition of malonyl-[acyl-carrier-protein]-decarboxylation Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.41 additional information
-
 additional information
-
 Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.3.1.86 soluble
-
 Escherichia coli
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.3.1.38 additional information high ionic strength required for maximal activity Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.1.39 35000
-
 1 * 35000, SDS-PAGE, alkylated: 1 * 35500, SDS-PAGE, native: 1 * 36500, SDS-PAGE Escherichia coli
2.3.1.39 35500
-
 1 * 35000, SDS-PAGE, alkylated: 1 * 35500, SDS-PAGE, native: 1 * 36500, SDS-PAGE Escherichia coli
2.3.1.39 36500
-
 1 * 35000, SDS-PAGE, alkylated: 1 * 35500, SDS-PAGE, native: 1 * 36500, SDS-PAGE Escherichia coli
2.3.1.39 36660
-
 carboxymethylated enzyme: sedimentation equilibrium centrifugation Escherichia coli
2.3.1.41 35000
-
 2 * 35000, SDS-PAGE Escherichia coli
2.3.1.41 37000
-
 2 * 37000, gel filtration after 6 M guanidinium chloride treatment Escherichia coli
2.3.1.41 66000
-
 equilibrium centrifugation Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.41 acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] Escherichia coli part of non-associated fatty acid synthase system of plants and prokaryotes 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
 ?
2.3.1.41 acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] Clostridium kluyveri part of non-associated fatty acid synthase system of plants and prokaryotes 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
 ?
2.3.1.41 acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] Escherichia coli responsible for chain elongation during de novo fatty acid synthesis 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
 ?
2.3.1.41 acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] Clostridium kluyveri responsible for chain elongation during de novo fatty acid synthesis 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.38 Escherichia coli
-
-
-
2.3.1.39 Escherichia coli
-
-
-
2.3.1.41 Clostridium kluyveri
-
-
-
2.3.1.41 Escherichia coli
-
-
-
2.3.1.85 Columba sp.
-
 pigeon
-
2.3.1.85 Rattus norvegicus
-
-
-
2.3.1.86 Escherichia coli
-
-
-
2.3.1.86 Euglena gracilis
-
-
-
2.3.1.86 Mycolicibacterium phlei
-
-
-
2.3.1.86 Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.39
-
 Escherichia coli
2.3.1.41
-
 Escherichia coli
2.3.1.86 purification of acyl carrier protein Escherichia coli

Reaction

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
a
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
a
2.3.1.85 acetyl-CoA + 7 malonyl-CoA + 14 NADPH + 14 H+ = hexadecanoate + 8 CoA + 7 CO2 + 14 NADP+ + 6 H2O reaction mechanism Rattus norvegicus
a
2.3.1.85 acetyl-CoA + 7 malonyl-CoA + 14 NADPH + 14 H+ = hexadecanoate + 8 CoA + 7 CO2 + 14 NADP+ + 6 H2O reaction mechanism Columba sp.
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.3.1.85 liver
-
 Rattus norvegicus
-
2.3.1.85 liver
-
 Columba sp.
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.3.1.38 0.06
-
-
 Escherichia coli
2.3.1.41 14
-
-
 Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.38 acetyl-CoA + [acyl-carrier protein] via acetyl-enzyme intermediate Escherichia coli CoA + acetyl-[acyl-carrier protein]
-
 r
2.3.1.38 acetyl-CoA + [acyl-carrier protein] pantetheine, not 2-mercaptoethanol can replace [acyl-carrier-protein] Escherichia coli CoA + acetyl-[acyl-carrier protein]
-
 r
2.3.1.38 acetyl-CoA + [acyl-carrier protein] acetyl-S-pantetheine can replace acetyl-CoA Escherichia coli CoA + acetyl-[acyl-carrier protein]
-
 r
2.3.1.38 butyryl-CoA + [acyl-carrier protein] 9.8% activity of that with acetyl-CoA Escherichia coli CoA + butyryl-[acyl-carrier protein]
-
 ?
2.3.1.38 hexanoyl-CoA + [acyl-carrier protein] 4.6% activity of that with acetyl-CoA Escherichia coli CoA + hexanoyl-[acyl-carrier protein]
-
 ?
2.3.1.38 additional information no substrate: malonyl-CoA Escherichia coli ?
-
 ?
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 propionyl-CoA + [acyl-carrier protein] transacylation at 23.4% the rate of acetyl-CoA Escherichia coli CoA + propionyl-[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 + N-(N-acetyl-beta-alanyl)cysteamine
-
 Escherichia coli CoA + N-(N-acetyl-beta-alanyl)-S-malonylcysteamine
-
 ?
2.3.1.39 malonyl-CoA + N-acetylcysteamine
-
 Escherichia coli CoA + N-acetyl-S-malonylcysteamine
-
 ?
2.3.1.39 malonyl-CoA + pantetheine
-
 Escherichia coli malonyl-pantetheine + CoA
-
 ?
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 acyl-CoA + [acyl-carrier protein] catalyzes fatty acyl transfer between CoA and [acyl-carrier-protein], but no direct transfer to the enzyme as with acyl-[acyl-carrier-protein] Escherichia coli acyl-[acyl-carrier protein] + CoA
-
 ?
2.3.1.41 acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] part of non-associated fatty acid synthase system of plants and prokaryotes Escherichia coli 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
 ?
2.3.1.41 acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] part of non-associated fatty acid synthase system of plants and prokaryotes Clostridium kluyveri 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
 ?
2.3.1.41 acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] responsible for chain elongation during de novo fatty acid synthesis Escherichia coli 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
 ?
2.3.1.41 acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] responsible for chain elongation during de novo fatty acid synthesis Clostridium kluyveri 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
 ?
2.3.1.41 cis-9-hexadecenoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
-
 Escherichia coli 3-oxo-cis-11-octadecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
 ?
2.3.1.41 cis-mono-unsaturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
-
 Clostridium kluyveri cis-mono-unsaturated 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
 ?
2.3.1.41 cis-mono-unsaturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] not cis-vaccenoyl-[acyl-carrier-protein], i.e. cis-11-octenoyl-[acyl-carrier-protein] Escherichia coli cis-mono-unsaturated 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
 ?
2.3.1.41 decanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
-
 Escherichia coli dodecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
 ?
2.3.1.41 dodecanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
-
 Escherichia coli 3-oxotetradecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
 ?
2.3.1.41 malonyl-[acyl-carrier protein] decarboxylation with 2-3% the rate of beta-ketoacyl-[acyl-carrier-protein]-synthesis Escherichia coli acetyl-[acyl-carrier protein] + CO2
-
 ?
2.3.1.41 saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
-
 Clostridium kluyveri 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
 ?
2.3.1.41 saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] substrate specificity, overview Escherichia coli 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]
-
 ?
2.3.1.41 tetradecanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
-
 Escherichia coli 3-oxohexadecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
 ?
2.3.1.85 additional information fatty acid synthetases of vertebrates and yeast are stable enzyme complexes of multifunctional polypeptide chains, the fatty acid synthetases of plants and E. coli consist of non-associated individual enzymes Rattus norvegicus ?
-
 ?
2.3.1.85 additional information fatty acid synthetases of vertebrates and yeast are stable enzyme complexes of multifunctional polypeptide chains, the fatty acid synthetases of plants and E. coli consist of non-associated individual enzymes Columba sp. ?
-
 ?
2.3.1.86 additional information fatty acid synthetases of vertebrates and yeast are stable enzyme complexes of multifunctional polypeptide chains, the fatty acid synthetases of plants and E. coli consist of non-associated individual enzymes Escherichia coli ?
-
 ?
2.3.1.86 additional information fatty acid synthetases of vertebrates and yeast are stable enzyme complexes of multifunctional polypeptide chains, the fatty acid synthetases of plants and E. coli consist of non-associated individual enzymes Saccharomyces cerevisiae ?
-
 ?

Subunits

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
2.3.1.39 monomer 1 * 35000, SDS-PAGE, alkylated: 1 * 35500, SDS-PAGE, native: 1 * 36500, SDS-PAGE Escherichia coli
2.3.1.39 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 * 35000, SDS-PAGE Escherichia coli
2.3.1.41 dimer 2 * 37000, gel filtration after 6 M guanidinium chloride treatment 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
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 Clostridium kluyveri
2.3.1.85 More
-
 Columba sp.
2.3.1.85 More fatty acid synthetases of vertebrates and yeast are stable enzyme complexes of multifunctional polypeptide chains, the fatty acid synthetases of plants and Escherichia coli consist of non-associated individual enzymes Rattus norvegicus
2.3.1.86 More
-
 Euglena gracilis
2.3.1.86 More fatty acid synthetases of vertebrates and yeast are stable enzyme complexes of multifunctional polypeptide chains, the fatty acid synthetases of plants and Escherichia coli consist of non-associated individual enzymes Escherichia coli
2.3.1.86 More fatty acid synthetases of vertebrates and yeast are stable enzyme complexes of multifunctional polypeptide chains, the fatty acid synthetases of plants and Escherichia coli consist of non-associated individual enzymes Saccharomyces cerevisiae

Synonyms

EC Number Synonyms Comment Organism
2.3.1.39 More in vertebrates, yeast and mycobacteria malonyl 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
2.3.1.41 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
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 Clostridium kluyveri

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.38 6.5
-
-
 Escherichia coli
2.3.1.39 6.5 8.5
-
 Escherichia coli
2.3.1.41 7 7.8
-
 Escherichia coli

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.3.1.41 6.5 8
-
 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
2.3.1.86 NADPH
-
 Saccharomyces cerevisiae
2.3.1.86 NADPH
-
 Mycolicibacterium phlei