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Literature summary extracted from

  • Bergler, H.; Fuchsbichler, S.; Hoegenauer, G.; Turnowsky, F.
    The enoyl-[acyl-carrier-protein] reductase (FabI) of Escherichia coli, which catalyzes a key regulatory step in fatty acid biosynthesis, accepts NADH and NADPH as cofactors and is inhibited by palmitoyl-CoA (1996), Eur. J. Biochem., 242, 689-694.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.1.10 fabI in pUC118 Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
1.3.1.10 G93S leads to diazaborine resistance Salmonella enterica subsp. enterica serovar Typhimurium
1.3.1.10 G93S leads to diazaborine resistance Escherichia coli
1.3.1.10 S241F leads to temperature sensitive growth and abolished activity Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.3.1.9 6-methyl-2-(propane-1-sulfonyl)-4a,7a-dihydro-2H-thieno[3,2-d][1,2,3]diazaborinin-1-ol diazaborine derviative 2b18, 90% loss of NADH-dependent activity, 50% loss of NADPH-dependent activity at 0.52 mM Escherichia coli
1.3.1.9 palmitoyl-CoA 50% inhibition at 0.0054 mM, competitive inhibition Escherichia coli
1.3.1.10 6-methyl-2-(propane-1-sulfonyl)-4a,7a-dihydro-2H-thieno[3,2-d][1,2,3]diazaborinin-1-ol diazaborine derivative 2b18, binds only in presence of NADH or NADPH, non-competitive inhibition, 0.2 mM lead to 25% inhibition, 0.52 mM to 50%, 1.56 mM to 80%. Increasing the inhibitor concentrations lead to preference for shorter acyl chain lengths Escherichia coli
1.3.1.10 palmitoyl-CoA 0.0016 mM lead to 50% inhibition, 0.002 mM to 60%, 0.005 mM to 20%, 0.01 mM to nearly total inhibition Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.3.1.9 33000
-
 monomeric form, SDS-PAGE Escherichia coli
1.3.1.10 33000
-
 FabI, SDS-PAGE Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.1.10 additional information Salmonella enterica subsp. enterica serovar Typhimurium part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters ?
-
 ?
1.3.1.10 additional information Escherichia coli part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.3.1.9 Escherichia coli
-
 wild type and temperature sensitive mutants
-
1.3.1.10 Escherichia coli
-
-
-
1.3.1.10 Salmonella enterica subsp. enterica serovar Typhimurium
-
 as there is no information concerning the stereochemistry of hydrogen transfer from NADPH to substrate an appointment to EC 1.3.1.10 or EC 1.3.1.39 is impossible
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.1.9
-
 Escherichia coli
1.3.1.10 in BisTris puffer pH 6.5 in order to retain NADPH dependent activity which is lost at pH 7.5 Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.3.1.9 additional information
-
 specific activities in temperature sensitive mutants Escherichia coli
1.3.1.10 0.008
-
 crude cell extract Escherichia coli
1.3.1.10 0.4
-
 purified by chromatography on DEAE-cellulose and Blue sepharose Escherichia coli

Storage Stability

EC Number Storage Stability Organism
1.3.1.10 -20°C, rapidly inactivated Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.1.9 additional information enzyme uses as well NADH as NADPH Escherichia coli ?
-
 ?
1.3.1.10 additional information part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters Salmonella enterica subsp. enterica serovar Typhimurium ?
-
 ?
1.3.1.10 additional information part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters Escherichia coli ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.3.1.10 More NADPH dependent acyl-ACP reductase and NADH dependent acyl-ACP/acyl-CoA reductase activity reside on the same protein Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.1.9 NADH
-
 Escherichia coli
1.3.1.9 NADPH
-
 Escherichia coli
1.3.1.10 additional information enzyme also exhibits NADPH dependent activity, if isolated at pH 6.5 Escherichia coli

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.3.1.9 0.02
-
 palmitoyl-CoA
-
 Escherichia coli