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Literature summary for 1.3.1.9 extracted from

  • Lu, H.; Tonge, P.J.
    Mechanism and inhibition of the FabV enoyl-ACP reductase from Burkholderia mallei (2010), Biochemistry, 49, 1281-1289.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.3.1.9

Activating Compound

Activating Compound Comment Organism Structure
NaCl optimal oionic strength 0.62 mM Burkholderia mallei

Cloned(Commentary)

Cloned (Comment) Organism
-
 Burkholderia mallei
gene fabV, expression of His-tagged wild-type and mutant enzymes in Escherichia coli BL21(DE3), theN-terminal His-tag in bmFabv does not have a dramatic effect on catalytic activity Burkholderia mallei

Protein Variants

Protein Variants Comment Organism
K244A site-directed mutagenesis Burkholderia mallei
K244A mutation does not induce major structural alterations. 110fold decrease in kcat value Burkholderia mallei
K244A/K245A loss of activity Burkholderia mallei
K244A/K245A site-directed mutagenesis Burkholderia mallei
K244R site-directed mutagenesis Burkholderia mallei
K244R mutation does not induce major structural alterations. 950fold decrease in kcat value Burkholderia mallei
K245M site-directed mutagenesis Burkholderia mallei
K245M mutation does not induce major structural alterations. 3fold increase in Km value for substrate dodecanoyl-CoA, 70fold decrease in kcat for substrate reduction Burkholderia mallei
Y235A site-directed mutagenesis Burkholderia mallei
Y235A mutation does not induce major structural alterations. 280fold decrease in kcat/Km ratio Burkholderia mallei
Y235S site-directed mutagenesis Burkholderia mallei
Y235S mutation does not induce major structural alterations. 280fold decrease in kcat/Km ratio Burkholderia mallei

Inhibitors

Inhibitors Comment Organism Structure
triclosan a rapid, reversible inhibitor of bmFabV, and a competitive inhibitor with respect to NADH and an uncompetitive inhibitor with respect to the substrate 2-dodecenoyl-CoA. Triclosan binds to the enzyme-NAD+ product complex which is in rapid and reversible equilibrium with other intermediates on the reaction pathway; competitive inhibitor with respect to NADH and an uncompetitive inhibitor with respect to the substrate 2-dodecenoyl-CoA Burkholderia mallei

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Km for NADH of 0.023 mM, a Km for 2-dodecenoyl-CoA of 0.0025 mM, and a kcat of 20.7 s-1. Steady-state kinetics, overview Burkholderia mallei
0.0022
-
 (2E)-2-dodecenoyl-CoA mutant Y235S, pH 7.9, 25°C Burkholderia mallei
0.0027
-
 (2E)-2-dodecenoyl-CoA mutant Y235A, pH 7.9, 25°C Burkholderia mallei
0.0044
-
 (2E)-2-dodecenoyl-CoA wild-type, pH 7.9, 25°C Burkholderia mallei
0.006
-
 NADH mutant Y235S, pH 7.9, 25°C Burkholderia mallei
0.0072
-
 (2E)-2-dodecenoyl-CoA mutant K244A, pH 7.9, 25°C Burkholderia mallei
0.0075
-
 (2E)-2-dodecenoyl-CoA mutant K244R, pH 7.9, 25°C Burkholderia mallei
0.023
-
 NADH mutant Y235A, pH 7.9, 25°C Burkholderia mallei
0.023
-
 NADH wild-type, pH 7.9, 25°C Burkholderia mallei
0.025
-
 crotonyl-[acyl-carrier protein] pH 7.9, 25°C Burkholderia mallei
0.028
-
 NADH mutant K245M, pH 7.9, 25°C Burkholderia mallei
0.028
-
 (2E)-2-dodecenoyl-CoA mutant K245M, pH 7.9, 25°C Burkholderia mallei
0.066
-
 NADH mutant K244A, pH 7.9, 25°C Burkholderia mallei
0.069
-
 NADH mutant K244R, pH 7.9, 25°C Burkholderia mallei

Organism

Organism UniProt Comment Textmining
Burkholderia mallei Q62L02
-
-
Burkholderia mallei Q62L02 gene fabV
-
Burkholderia mallei ATCC 23344 Q62L02 gene fabV
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli BL21(DE3) by nickel affinity chromatography Burkholderia mallei

Reaction

Reaction Comment Organism Reaction ID
an acyl-[acyl-carrier protein] + NAD+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH + H+ detailed kinetic analysis of the sequential bi-bi mechanism with NADH binding first and NAD+ dissociating last. The catalytic tyrosine (Y235) and lysine (K244) residues are organized in the consensus Tyr-(Xaa)8-Lys motif. Both Y235 and K244 are involved in acid-base chemistry during substrate reduction Burkholderia mallei
a
an acyl-[acyl-carrier protein] + NAD+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH + H+ sequential Bi Bi mechanism with NADH binding first and NAD+ dissociating last Burkholderia mallei
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(2E)-2-dodecenoyl-CoA + NADH + H+
-
 Burkholderia mallei dodecanoyl-CoA + NAD+
-
 ?
(2E)-2-dodecenoyl-CoA + NADH + H+
-
 Burkholderia mallei ATCC 23344 dodecanoyl-CoA + NAD+
-
 ?
crotonyl-[acyl-carrier protein] + NAD+
-
 Burkholderia mallei ? + NADH + H+
-
 ?
crotonyl-[acyl-carrier protein] + NAD+
-
 Burkholderia mallei ATCC 23344 ? + NADH + H+
-
 ?
crotonyl-[acyl-carrier protein] + NADH
-
 Burkholderia mallei butyryl-[acyl-carrier protein] + NAD+
-
 ?
crotonyl-[acyl-carrier protein] + NADH
-
 Burkholderia mallei ATCC 23344 butyryl-[acyl-carrier protein] + NAD+
-
 ?
additional information activity measurement using NAD+ cofactor and substrate 2-dodecenoyl-CoA Burkholderia mallei ?
-
 ?
additional information activity measurement using NAD+ cofactor and substrate 2-dodecenoyl-CoA Burkholderia mallei ATCC 23344 ?
-
 ?

Synonyms

Synonyms Comment Organism
BMA0885
-
 Burkholderia mallei
enoyl-ACP reductase
-
 Burkholderia mallei
FabV
-
 Burkholderia mallei
More the enzyme is a member of the short chain dehydrogenase/reductase superfamily Burkholderia mallei

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Burkholderia mallei

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.022
-
 (2E)-2-dodecenoyl-CoA mutant K244R, pH 7.9, 25°C Burkholderia mallei
0.08
-
 (2E)-2-dodecenoyl-CoA mutant Y235A, pH 7.9, 25°C Burkholderia mallei
0.1
-
 (2E)-2-dodecenoyl-CoA mutant Y235S, pH 7.9, 25°C Burkholderia mallei
0.18
-
 (2E)-2-dodecenoyl-CoA mutant K244A, pH 7.9, 25°C Burkholderia mallei
0.3
-
 (2E)-2-dodecenoyl-CoA mutant K245M, pH 7.9, 25°C Burkholderia mallei
28.8
-
 (2E)-2-dodecenoyl-CoA wild-type, pH 7.9, 25°C Burkholderia mallei

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.9
-
-
 Burkholderia mallei
7.9
-
 assay at Burkholderia mallei

pH Range

pH Minimum pH Maximum Comment Organism
6.6 8.5
-
 Burkholderia mallei

Cofactor

Cofactor Comment Organism Structure
NADH
-
 Burkholderia mallei

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
additional information
-
 additional information inhibition kinetics, overview Burkholderia mallei
0.0004
-
 triclosan versus 2-dodecenoyl-CoA, pH 7.8, 25°C Burkholderia mallei
0.0004
-
 triclosan substrate 2-dodecenoyl-CoA, pH 7.9, 25°C Burkholderia mallei

General Information

General Information Comment Organism
metabolism enoyl-ACP reductases catalyze the final step in the elongation cycle of the bacterial fatty acid biosynthesis, FAS-II, pathway, but FabV is distinct and belongs to another class of enoyl-acyl carrier protein reductases, overview Burkholderia mallei

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.011
-
 (2E)-2-dodecenoyl-CoA mutant K245M, pH 7.9, 25°C Burkholderia mallei
0.025
-
 (2E)-2-dodecenoyl-CoA mutant K244A, pH 7.9, 25°C Burkholderia mallei
0.028
-
 (2E)-2-dodecenoyl-CoA mutant K244R, pH 7.9, 25°C Burkholderia mallei
0.03
-
 (2E)-2-dodecenoyl-CoA mutant Y235A, pH 7.9, 25°C Burkholderia mallei
0.047
-
 (2E)-2-dodecenoyl-CoA mutant Y235S, pH 7.9, 25°C Burkholderia mallei
6.5
-
 (2E)-2-dodecenoyl-CoA wild-type, pH 7.9, 25°C Burkholderia mallei