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Literature summary for 6.4.1.2 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
Search for more literature for 6.4.1.2

Cloned(Commentary)

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

Protein Variants

Protein Variants Comment Organism
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
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]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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

Metals/Ions Comment Organism Structure
Mg2+
-
 Streptomyces coelicolor

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Streptomyces coelicolor
-
-
-

Posttranslational Modification

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

Reaction

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + acetyl-CoA + HCO3-
-
 Streptomyces coelicolor ADP + malonyl-CoA + phosphate
-
 ?
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
-
 ?
ATP + butyryl-CoA + HCO3- + H+ wild-type enzyme Streptomyces coelicolor ADP + glutaryl-CoA + phosphate
-
 ?
ATP + propionyl-CoA + HCO3- + H+ wild-type and mutant I420D enzyme Streptomyces coelicolor ADP + succinyl-CoA + phosphate
-
 ?

Subunits

Subunits Comment Organism
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

Synonyms Comment Organism
ACC
-
 Streptomyces coelicolor
ACCase
-
 Streptomyces coelicolor

pH Optimum

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

Cofactor

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