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Literature summary extracted from

  • Diacovich, L.; Mitchell, D.L.; Pham, H.; Gago, G.; Melgar, M.M.; Khosla, C.; Gramajo, H.; Tsai, S.C.
    Crystal structure of the beta-subunit of acyl-CoA carboxylase: structure-based engineering of substrate specificity (2004), Biochemistry, 43, 14027-14036.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.4.1.2 expression of subunits AccA2, AccB, and AccE, and of mutant AccB in Escherichia coli Streptomyces coelicolor

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.4.1.3 apo and substrate-bound crystal structure of PccB hexamers determined to 2.0-2.8 A. crystallization of PccB in sitting drops at room temperature by vapor diffusion. PccB is the core catalytic beta subunit of the propanoyl-CoA carboxylase multisubunit complex Streptomyces coelicolor

Protein Variants

EC Number Protein Variants Comment Organism
6.4.1.2 I420D site-directed mutagenesis of AccB, exchange of a single amino acid results in interconversion of substrate specificity of acetyl-CoA carboxylase ACC and propionyl-CoA carboxylase, PCC, EC 6.4.1.3, thus the mutant enzyme does not utilize acetyl-CoA as a substrate, but propionyl-CoA Streptomyces coelicolor
6.4.1.2 additional information formation of chimeric complexes with subunits, wild-type and mutant D422I, of the propionyl-CoA carboxylase, PCC, EC 6.4.1.3, and with mutant subunit AccB I420D of the acetyl-CoA carboxylase Streptomyces coelicolor

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.4.1.2 additional information
-
 additional information kinetics of chimeric complexes of wild-type and mutant propionyl-CoA carboxylase, EC 6.4.1.3, subunits and acetyl-CoA carboxylase subunits Streptomyces coelicolor

Metals/Ions

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

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.4.1.2 ATP + acetyl-CoA + HCO3- Streptomyces coelicolor
-
 ADP + malonyl-CoA + phosphate
-
 ?

Organism

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

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
6.4.1.2 additional information the enzyme is biotinylated Streptomyces coelicolor

Purification (Commentary)

EC Number Purification (Comment) Organism
6.4.1.3 recombinant Streptomyces coelicolor

Reaction

EC Number Reaction Comment Organism Reaction ID
6.4.1.2 ATP + acetyl-CoA + hydrogencarbonate = ADP + phosphate + malonyl-CoA substrate specificity, catalytic mechanism, and structural features Streptomyces coelicolor
a

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
-
 ?
6.4.1.2 ATP + acetyl-CoA + HCO3- wild-type enzyme, transcarboxylation between biotin and acetyl-CoA is catalyzed by the core catalytic beta-subunit Streptomyces coelicolor ADP + malonyl-CoA + phosphate
-
 ?
6.4.1.2 ATP + butyryl-CoA + HCO3- + H+ wild-type enzyme Streptomyces coelicolor ADP + glutaryl-CoA + phosphate
-
 ?
6.4.1.2 ATP + propionyl-CoA + HCO3- + H+ wild-type and mutant I420D enzyme Streptomyces coelicolor ADP + succinyl-CoA + phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
6.4.1.2 More the core catalytic beta-subunit is a homohexameric complex of 360 kDa, structure overview, the dimeric interaction is crucial for enzyme catalysis, stability, and substrate specificity, interaction between alpha- and beta-subunits, overview Streptomyces coelicolor

Synonyms

EC Number Synonyms Comment Organism
6.4.1.2 ACC
-
 Streptomyces coelicolor
6.4.1.2 ACCase
-
 Streptomyces coelicolor
6.4.1.3 PCC
-
 Streptomyces coelicolor

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.4.1.2 7.6
-
 assay at Streptomyces coelicolor

Cofactor

EC Number Cofactor Comment Organism Structure
6.4.1.2 ATP
-
 Streptomyces coelicolor
6.4.1.2 biotin transcarboxylation between biotin and acetyl-CoA catalyzed by the core catalytic beta-subunit Streptomyces coelicolor