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Literature summary for 1.3.1.10 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
Search for more literature for 1.3.1.10

Cloned(Commentary)

Cloned (Comment) Organism
fabI in pUC118 Escherichia coli

Protein Variants

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

Inhibitors

Inhibitors Comment Organism Structure
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
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]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
33000
-
 FabI, SDS-PAGE Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
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)

Purification (Comment) Organism
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]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.008
-
 crude cell extract Escherichia coli
0.4
-
 purified by chromatography on DEAE-cellulose and Blue sepharose Escherichia coli

Storage Stability

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

Substrates and Products (Substrate)

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

Synonyms

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

Cofactor

Cofactor Comment Organism Structure
additional information enzyme also exhibits NADPH dependent activity, if isolated at pH 6.5 Escherichia coli