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6.4.1.3: propionyl-CoA carboxylase

This is an abbreviated version!
For detailed information about propionyl-CoA carboxylase, go to the full flat file.

Word Map on EC 6.4.1.3

Reaction

ATP
+
propanoyl-CoA
+
HCO3-
+
H+
=
ADP
+
phosphate
+
(S)-methylmalonyl-CoA

Synonyms

AccA3-PccB complex, acetyl-CoA/propionyl-CoA carboxylase, Carboxylase, propional coenzyme A (adenosine triphosphate-hydrolyzing), LA_2736-LA_2735, Pcase, PCC, PccA, PccA-1, PCCase, PccB, PccB-1, pccBC, PccE, Propanoyl-CoA:carbon dioxide ligase, Propionyl coenzyme A carboxylase, Propionyl coenzyme A carboxylase (adenosine triphosphate-hydrolyzing), Propionyl coenzyme A carboxylase (ATP-hydrolyzing), Propionyl-CoA carboxylase, propionyl-coenzyme A carboxylase

ECTree

     6 Ligases
         6.4 Forming carbon-carbon bonds
             6.4.1 Ligases that form carbon-carbon bonds (only sub-subclass identified to date)
                6.4.1.3 propionyl-CoA carboxylase

Crystallization

Crystallization on EC 6.4.1.3 - propionyl-CoA carboxylase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
a PCC chimaera, containing the alpha-subunit of Ruegeria pomeroyi PCC and the beta-subunit of Roseobacter denitrificans PCC is crystallized by the microbatch method under paraffin oil, using 0.1 M HEPES (pH 8.0), 22% (w/v) PEG3350, 0.2 M NaCl and 16% (v/v) glycerol. Crystals of Ruegeria pomeroyi PCC are obtained at 20°C by the microbatch method under paraffin oil, using 0.2 M succinic acid (pH 6.5), 22% (w/v) benzamidine and 22% (w/v) PEG3000
microbatch method under oil method
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
-
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