Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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)

EC Number Cloned (Comment) Organism
6.4.1.2 expressed in Escherichia coli BL21 lambda(DE3) cells Streptomyces coelicolor
6.4.1.3 expressed in Escherichia coli BL21 lambda(DE3) cells Streptomyces coelicolor

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.4.1.3 sitting drop vapor diffusion method, mutant enzymes D422V and D422Lwith 0.1 M Tris pH 6.5, 2.0 M (NH4)SO4, mutant enzyme D422N with 0.1 M Bis-Tris pH 6.8, 10% (w/v) MPD, 0.2 M (NH4)OAc, mutant enzyme D422C with 0.1 M Na citrate pH 5.6, 0.2 M (NH4)SO4, and mutant enzyme D422A with 0.1 M Bis-Tris pH 6.2, 20% (w/v) PEG3350, 0.2 M (NH4)SO4 Streptomyces coelicolor

Protein Variants

EC Number Protein Variants Comment Organism
6.4.1.3 D422A mutant of the PccB subunit, shows strong preference for butyryl-CoA as substrate Streptomyces coelicolor
6.4.1.3 D422C mutant of the PccB subunit, shows strong preference for butyryl-CoA as substrate Streptomyces coelicolor
6.4.1.3 D422I mutant of the PccB subunit, accepts acetyl-CoA, propionyl-CoA, and butyrl-CoA as substrates, the latter two with lower Vmax/Km values as compared to the wild type enzyme Streptomyces coelicolor
6.4.1.3 D422L mutant of the PccB subunit, the mutants has narrowed down their substrate specificity, accepting only propionyl-CoA as its substrate Streptomyces coelicolor
6.4.1.3 D422N mutant of the PccB subunit, the mutants has narrowed down their substrate specificity, accepting only propionyl-CoA as its substrate Streptomyces coelicolor
6.4.1.3 D422V mutant of the PccB subunit, accepts both propionyl-CoA and butyrl-CoA as substrates but with lower Vmax/Km values as compared to the wild type enzyme Streptomyces coelicolor

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.4.1.2 0.092
-
 propionyl-CoA wild type subunit AccB, in 100 mM potassium phosphate, pH 7.6, at 30°C Streptomyces coelicolor
6.4.1.2 0.099
-
 butyryl-CoA wild type subunit AccB, in 100 mM potassium phosphate, pH 7.6, at 30°C Streptomyces coelicolor
6.4.1.2 0.1
-
 acetyl-CoA wild type subunit AccB, in 100 mM potassium phosphate, pH 7.6, at 30°C Streptomyces coelicolor
6.4.1.3 0.036
-
 butyryl-CoA mutant enzyme D422C, in 100 mM potassium phosphate, pH 7.6, at 30°C Streptomyces coelicolor
6.4.1.3 0.056
-
 propionyl-CoA mutant enzyme D422C, in 100 mM potassium phosphate, pH 7.6, at 30°C Streptomyces coelicolor
6.4.1.3 0.059
-
 butyryl-CoA mutant enzyme D422A, in 100 mM potassium phosphate, pH 7.6, at 30°C Streptomyces coelicolor
6.4.1.3 0.076
-
 propionyl-CoA wild type enzyme, in 100 mM potassium phosphate, pH 7.6, at 30°C Streptomyces coelicolor
6.4.1.3 0.077
-
 propionyl-CoA mutant enzyme D422V, in 100 mM potassium phosphate, pH 7.6, at 30°C Streptomyces coelicolor
6.4.1.3 0.104
-
 butyryl-CoA wild type enzyme, in 100 mM potassium phosphate, pH 7.6, at 30°C Streptomyces coelicolor
6.4.1.3 0.123
-
 propionyl-CoA mutant enzyme D422N, in 100 mM potassium phosphate, pH 7.6, at 30°C Streptomyces coelicolor
6.4.1.3 0.159
-
 propionyl-CoA mutant enzyme D422L, in 100 mM potassium phosphate, pH 7.6, at 30°C Streptomyces coelicolor
6.4.1.3 0.262
-
 propionyl-CoA mutant enzyme D422A, in 100 mM potassium phosphate, pH 7.6, at 30°C Streptomyces coelicolor
6.4.1.3 0.315
-
 propionyl-CoA mutant enzyme D422I, in 100 mM potassium phosphate, pH 7.6, at 30°C Streptomyces coelicolor
6.4.1.3 0.317
-
 butyryl-CoA mutant enzyme D422I, in 100 mM potassium phosphate, pH 7.6, at 30°C Streptomyces coelicolor
6.4.1.3 0.335
-
 acetyl-CoA mutant enzyme D422I, in 100 mM potassium phosphate, pH 7.6, at 30°C Streptomyces coelicolor
6.4.1.3 0.383
-
 butyryl-CoA mutant enzyme D422V, in 100 mM potassium phosphate, pH 7.6, at 30°C Streptomyces coelicolor

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.4.1.2 Mg2+ required Streptomyces coelicolor

Organism

EC Number Organism UniProt Comment Textmining
6.4.1.2 Streptomyces coelicolor
-
-
-
6.4.1.3 Streptomyces coelicolor Q9X4K7
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.4.1.2
-
 Streptomyces coelicolor
6.4.1.3 nickel affinity column chromatography Streptomyces coelicolor

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.4.1.2 ATP + acetyl-CoA + HCO3-
-
 Streptomyces coelicolor ADP + malonyl-CoA + phosphate
-
 r
6.4.1.2 ATP + butyryl-CoA + HCO3-
-
 Streptomyces coelicolor ADP + ethylmalonyl-CoA + phosphate
-
 r
6.4.1.2 ATP + propionyl-CoA + HCO3-
-
 Streptomyces coelicolor ADP + methylmalonyl-CoA + phosphate
-
 r
6.4.1.3 acetyl-CoA + CO2 the wild type enzyme shows no activity with acetyl-CoA, but mutant enzyme D422I does Streptomyces coelicolor ?
-
 ?
6.4.1.3 butyryl-CoA + CO2
-
 Streptomyces coelicolor ?
-
 ?
6.4.1.3 additional information the wild type enzyme shows no activity with acetyl-CoA Streptomyces coelicolor ?
-
 ?
6.4.1.3 propionyl-CoA + CO2
-
 Streptomyces coelicolor (S)-methylmalonyl-CoA
-
 ?

Synonyms

EC Number Synonyms Comment Organism
6.4.1.2 ACC
-
 Streptomyces coelicolor
6.4.1.2 ACCase the ACCase that preferentially accepts acetyl-CoA as a substrate is defined as an acetyl-CoA carboxylase (ACC) Streptomyces coelicolor
6.4.1.2 ACCB subunit Streptomyces coelicolor
6.4.1.3 PCC
-
 Streptomyces coelicolor
6.4.1.3 PccB beta-subunit Streptomyces coelicolor
6.4.1.3 PccE epsilon-subunit Streptomyces coelicolor
6.4.1.3 Propionyl-CoA carboxylase
-
 Streptomyces coelicolor

Cofactor

EC Number Cofactor Comment Organism Structure
6.4.1.2 ATP
-
 Streptomyces coelicolor
6.4.1.2 biotin
-
 Streptomyces coelicolor
6.4.1.3 biotin
-
 Streptomyces coelicolor