Literature summary for 6.4.1.3 extracted from

Huang, C.; Sadre-Bazzaz, K.; Shen, Y.; Deng, B.; Zhou, Z.; Tong, L.
Crystal structure of the alpha6beta6 holoenzyme of propionyl-coenzyme A carboxylase (2010), Nature, 466, 1001-1005.

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli	Ruegeria pomeroyi

Crystallization (Commentary)

Crystallization (Comment)	Organism
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	Ruegeria pomeroyi
microbatch method under oil method	Ruegeria pomeroyi

Crystallization (Comment)

Organism

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

Ruegeria pomeroyi

microbatch method under oil method

Ruegeria pomeroyi

Protein Variants

Protein Variants	Comment	Organism
D440I	the mutation does not change the substrate preference of the enzyme	Ruegeria pomeroyi
G668R	the mutation in the biotin carboxyl carrier protein domain abolishes biotinylation	Ruegeria pomeroyi
R165Q	the mutation disturbs the recognition of the adenine base of CoA	Ruegeria pomeroyi
R165W	the mutation disturbs the recognition of the adenine base of CoA	Ruegeria pomeroyi
R399Q	the mutation leads to a large loss in activity	Ruegeria pomeroyi

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
mitochondrion	-	Ruegeria pomeroyi	5739	-

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
750000	-	-	Ruegeria pomeroyi
750000	-	gel filtration	Ruegeria pomeroyi

Organism

Organism	UniProt	Comment	Textmining
Ruegeria pomeroyi	-	-	-
Ruegeria pomeroyi	Q5LUF3	-	-

Purification (Commentary)

Purification (Comment)	Organism
nickel affinity column chromatography and gel filtration	Ruegeria pomeroyi

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
acetyl-CoA + CO2	the enzyme has a preference for propionyl-CoA over acetyl-CoA as the substrate	Ruegeria pomeroyi	?	-	?
ATP + acetyl-CoA + HCO3-	the enzyme has a preference for propanoyl-CoA over acetyl-CoA as the substrate	Ruegeria pomeroyi	ADP + phosphate + malonyl-CoA	-	?
ATP + propanoyl-CoA + HCO3-	the enzyme has a preference for propanoyl-CoA over acetyl-CoA as the substrate	Ruegeria pomeroyi	ADP + phosphate + (S)-methylmalonyl-CoA	-	?
propionyl-CoA + CO2	the enzyme has a preference for propionyl-CoA over acetyl-CoA as the substrate	Ruegeria pomeroyi	(S)-methylmalonyl-CoA	-	?

Subunits

Subunits	Comment	Organism
heterododecamer	alpha6beta6-heterododecamer, the alpha-subunit contains the biotin carboxylase and biotin carboxyl carrier protein domains, whereas the beta-subunit supplies the carboxyltransferase activity	Ruegeria pomeroyi
heterododecamer	the alpha-subunit contains the biotin carboxylase and biotin carboxyl carrier protein domains, whereas the beta-subunit supplies the carboxyltransferase activity	Ruegeria pomeroyi

Synonyms

Synonyms	Comment	Organism
PCC	-	Ruegeria pomeroyi
propionyl-coenzyme A carboxylase	-	Ruegeria pomeroyi

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Ruegeria pomeroyi
biotin	-	Ruegeria pomeroyi

General Information

General Information	Comment	Organism
metabolism	PCC is essential for the catabolism of the amino acids L-Thr, L-Val, L-Ile and L-Met, cholesterol and fatty acids with an odd number of carbon atoms	Ruegeria pomeroyi