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Literature summary for 1.3.8.8 extracted from

  • Tani, A.; Ishige, T.; Sakai, Y.; Kato, N.
    Two acyl-CoA dehydrogenases of Acinetobacter sp. strain M-1 that uses very long-chain n-alkanes (2002), J. Biosci. Bioeng., 94, 326-329.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene acdB, DNA and amino acid sequence determination and analysis, genes acdA and acdB are arranged in a tandem, expression of gene acdB in Escherichia coli strain JM109 Acinetobacter sp.

Inhibitors

Inhibitors Comment Organism Structure
Ag+ 1 mM, complete inhibition of the recombinant enzyme Acinetobacter sp.
Cu2+ 1 mM, complete inhibition of the recombinant enzyme Acinetobacter sp.
Hg2+ 1 mM, 61% inhibition of the recombinant enzyme Acinetobacter sp.
Mn2+ 1 mM, 72% inhibition of the recombinant enzyme Acinetobacter sp.
Pb2+ 1 mM, 23% inhibition of the recombinant enzyme Acinetobacter sp.
Zn2+ 1 mM, 19% inhibition of the recombinant enzyme Acinetobacter sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.068
-
lauroyl-CoA pH 8.5, recombinant enzyme Acinetobacter sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
64000
-
2 * 64833, amino acid sequence determination, 2 * 64000, recombinant enzyme, SDS-PAGE Acinetobacter sp.
64833
-
2 * 64833, amino acid sequence determination, 2 * 64000, recombinant enzyme, SDS-PAGE Acinetobacter sp.
135000
-
recombinant enzyme, gel filtration Acinetobacter sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
lauroyl-CoA + acceptor Acinetobacter sp. enzyme shows preference for long-chain fatty acids 2-dodecenoyl-CoA + reduced acceptor
-
?
lauroyl-CoA + acceptor Acinetobacter sp. M-1 enzyme shows preference for long-chain fatty acids 2-dodecenoyl-CoA + reduced acceptor
-
?

Organism

Organism UniProt Comment Textmining
Acinetobacter sp. Q8L0X1 gene acdB
-
Acinetobacter sp. M-1 Q8L0X1 gene acdB
-

Purification (Commentary)

Purification (Comment) Organism
recombinant acdB-encoded enzyme from Escherichia coli Acinetobacter sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
lauroyl-CoA + acceptor enzyme shows preference for long-chain fatty acids Acinetobacter sp. 2-dodecenoyl-CoA + reduced acceptor
-
?
lauroyl-CoA + acceptor enzyme shows preference for long-chain fatty acids Acinetobacter sp. M-1 2-dodecenoyl-CoA + reduced acceptor
-
?

Subunits

Subunits Comment Organism
dimer 2 * 64833, amino acid sequence determination, 2 * 64000, recombinant enzyme, SDS-PAGE Acinetobacter sp.

Synonyms

Synonyms Comment Organism
AcdB
-
Acinetobacter sp.

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
purified recombinant enzyme, 30 min, 80% remaining activity Acinetobacter sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
-
Acinetobacter sp.

pH Stability

pH Stability pH Stability Maximum Comment Organism
8 10 recombinant enzyme Acinetobacter sp.

Cofactor

Cofactor Comment Organism Structure
FAD 1 mol per mol of subunit, participates directly in the catalytic reaction Acinetobacter sp.