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Literature summary for 6.3.4.14 extracted from

  • Weatherly, S.C.; Volrath, S.L.; Elich, T.D.
    Expression and characterization of recombinant fungal acetyl-CoA carboxylase and isolation of a soraphen-binding domain (2004), Biochem. J., 380, 105-110.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
truncated biotin carboxylase domain of acetyl-CoA carboxylase, expression in Escherichia coli Ustilago maydis
truncated biotin carboxylase domain of acetyl-CoA carboxylase, expression in Escherichia coli Pyricularia grisea
truncated biotin carboxylase domain of acetyl-CoA carboxylase, expression in Escherichia coli Phytophthora infestans

General Stability

General Stability Organism
the truncated biotin carboxylase domain is more stable than the full-length enzyme Ustilago maydis

Inhibitors

Inhibitors Comment Organism Structure
soraphen
-
Phytophthora infestans
soraphen
-
Pyricularia grisea
soraphen
-
Ustilago maydis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
64700
-
x * 64700, recombinant biotin carboxylase domain Ustilago maydis

Organism

Organism UniProt Comment Textmining
Phytophthora infestans
-
-
-
Pyricularia grisea
-
-
-
Ustilago maydis
-
-
-

Subunits

Subunits Comment Organism
? x * 64700, recombinant biotin carboxylase domain Ustilago maydis