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Literature summary for 1.3.1.10 extracted from

  • Heath, R.J.; Li, J.; Roland, G.E.; Rock, C.O.
    Inhibition of the Staphylococcus aureus NADPH-dependent enoyl-acyl carrier protein reductase by triclosan and hexachlorophene (2000), J. Biol. Chem., 275, 4654-4659.
    View publication on PubMed
Search for more literature for 1.3.1.10

Cloned(Commentary)

Cloned (Comment) Organism
fabI of strain RN4220 found by homology and cloned into pET15b for his-tagged overexpression Staphylococcus aureus

Protein Variants

Protein Variants Comment Organism
G93V leads to triclosan resistance Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
Hexachlorophene half-maximal inhibition at 0.004 mM Staphylococcus aureus
triclosan half-maximal inhibition at 0.003 mM; slow-binding inhibitor forms a stable, ternary complex with enzyme and NADP+ Staphylococcus aureus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 NADPH value above 2 mM Escherichia coli
additional information
-
 NADPH half-maximal rate at 0.065 mM NADPH Staphylococcus aureus
additional information
-
 NADPH cooperative binding with Hill coefficient 2.2 Staphylococcus aureus
8
-
 Crotonyl-N-acetyl-cysteamine Vmax 0.0003 nmol/min/mg Staphylococcus aureus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Staphylococcus aureus 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
-
-
-
Staphylococcus aureus Q9RMI3 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
Ni2+ affinity chromatography on his-tagged protein Staphylococcus aureus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
crotonyl-N-acetyl-cysteamine + NADPH
-
 Staphylococcus aureus butyryl-N-acetyl-cysteamine + NADP+
-
 ?
additional information part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters Staphylococcus aureus ?
-
 ?
additional information part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters Escherichia coli ?
-
 ?
octenoyl-N-acetyl-cysteamine + NADPH
-
 Staphylococcus aureus octanoyl-N-acetyl-cysteamine + NADP+
-
 ?

Cofactor

Cofactor Comment Organism Structure
additional information enzyme is highly specific for NADH, even if isolated at pH 6.5 Escherichia coli