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Literature summary for 6.4.1.2 extracted from

  • Arabolaza, A.; Shillito, M.E.; Lin, T.W.; Diacovich, L.; Melgar, M.; Pham, H.; Amick, D.; Gramajo, H.; Tsai, S.C.
    Crystal structures and mutational analyses of acyl-CoA carboxylase beta subunit of Streptomyces coelicolor (2010), Biochemistry, 49, 7367-7376.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21 lambda(DE3) cells Streptomyces coelicolor

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.092
-
propionyl-CoA wild type subunit AccB, in 100 mM potassium phosphate, pH 7.6, at 30°C Streptomyces coelicolor
0.099
-
butyryl-CoA wild type subunit AccB, in 100 mM potassium phosphate, pH 7.6, at 30°C Streptomyces coelicolor
0.1
-
acetyl-CoA wild type subunit AccB, in 100 mM potassium phosphate, pH 7.6, at 30°C Streptomyces coelicolor

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Streptomyces coelicolor

Organism

Organism UniProt Comment Textmining
Streptomyces coelicolor
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Streptomyces coelicolor

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + acetyl-CoA + HCO3-
-
Streptomyces coelicolor ADP + malonyl-CoA + phosphate
-
r
ATP + butyryl-CoA + HCO3-
-
Streptomyces coelicolor ADP + ethylmalonyl-CoA + phosphate
-
r
ATP + propionyl-CoA + HCO3-
-
Streptomyces coelicolor ADP + methylmalonyl-CoA + phosphate
-
r

Synonyms

Synonyms Comment Organism
ACC
-
Streptomyces coelicolor
ACCase the ACCase that preferentially accepts acetyl-CoA as a substrate is defined as an acetyl-CoA carboxylase (ACC) Streptomyces coelicolor
ACCB subunit Streptomyces coelicolor

Cofactor

Cofactor Comment Organism Structure
ATP
-
Streptomyces coelicolor
biotin
-
Streptomyces coelicolor