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Literature summary for 1.3.1.10 extracted from

  • Heath, R.J.; Su, N.; Murphy, C.K.; Rock, C.O.
    The enoyl-[acyl-carrier-protein] reductases FabI and FabL from Bacillus subtilis (2000), J. Biol. Chem., 275, 40128-40133.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Bacillus subtilis
fabL in pET15b for his-tagged overexpression Bacillus subtilis

Protein Variants

Protein Variants Comment Organism
additional information the ygaA knockout is 250fold more sensitive to the inhibitor triclosan Bacillus subtilis

Inhibitors

Inhibitors Comment Organism Structure
triclosan half-maximal inhibition at 0.016 mM; reversible inhibitor that does not form a ternary complex; reversibly inhibited by, does not form the stable ternary complex characteristic of the FabI proteins. Expression of YgaA complements the fabI(ts) defect in Escherichia coli and conferrs complete triclosan resistance Bacillus subtilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.016
-
NADPH
-
Bacillus subtilis
0.016
-
NADPH no cooperativity in binding NADPH Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Bacillus subtilis part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters ?
-
?
additional information Bacillus subtilis catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters of both N-acetylcysteamine and acyl-carrier protein ?
-
?
additional information Bacillus subtilis 168 catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters of both N-acetylcysteamine and acyl-carrier protein ?
-
?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
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
-
Bacillus subtilis P71079
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni2+ affinity chromatography on his-tagged protein Bacillus subtilis
Ni2+ chelation chromatography Bacillus subtilis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.18
-
with octenyl-N-acetyl-cysteamine Bacillus subtilis
0.18
-
spectrophotometric assay, S-((2E)-oct-2-enoyl)-N-acetylcysteamine as a substrate Bacillus subtilis
0.3
-
with crotonyl-[acyl-carrier-protein] Bacillus subtilis
0.3
-
spectrophotometric assay, (2E)-but-2-enoyl-[acyl carrier protein] as a substrate Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(2E)-but-2-enoyl-[acyl carrier protein] + NADPH + H+
-
Bacillus subtilis butanoyl-[acyl-carrier protein] + NADP+
-
?
(2E)-but-2-enoyl-[acyl carrier protein] + NADPH + H+
-
Bacillus subtilis 168 butanoyl-[acyl-carrier protein] + NADP+
-
?
crotonyl-[acyl-carrier protein] + NADPH
-
Bacillus subtilis butyryl-[acyl-carrier protein] + NADP+
-
?
additional information part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters Bacillus subtilis ?
-
?
additional information catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters of both N-acetylcysteamine and acyl-carrier protein Bacillus subtilis ?
-
?
additional information catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters of both N-acetylcysteamine and acyl-carrier protein Bacillus subtilis 168 ?
-
?
octenoyl-N-acetyl-cysteamine + NADPH
-
Bacillus subtilis octanoyl-N-acetyl-cysteamine + NADP+
-
?
S-((2E)-oct-2-enoyl)-N-acetylcysteamine + NADPH + H+
-
Bacillus subtilis S-octanoyl-N-acetylcysteamine + NADP+
-
?
S-((2E)-oct-2-enoyl)-N-acetylcysteamine + NADPH + H+
-
Bacillus subtilis 168 S-octanoyl-N-acetylcysteamine + NADP+
-
?

Synonyms

Synonyms Comment Organism
enoyl-ACP reductase
-
Bacillus subtilis
FabL
-
Bacillus subtilis
YgaA
-
Bacillus subtilis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Bacillus subtilis

Cofactor

Cofactor Comment Organism Structure
NADPH inactive with NADH Bacillus subtilis

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.016
-
-
Bacillus subtilis triclosan

General Information

General Information Comment Organism
malfunction physiological function of the enzyme is examined by knocking out the gene and determining the effect of the gene disruptions on cell growth and triclosan sensitivity, the gene is not essential Bacillus subtilis