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Literature summary for 6.4.1.3 extracted from

  • Hou, J.; Xiang, H.; Han, J.
    Propionyl-CoA carboxylase in Haloferax mediterranei: indispensability for propionyl-CoA assimilation and impacts on global metabolism (2015), Appl. Environ. Microbiol., 81, 794-804.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.4.1.3

Organism

Organism UniProt Comment Textmining
Haloferax mediterranei I3R7G3 and I3R7F1 and I3R7F2 I3R7G3: biotin carboxylase subunit (PccA), I3R7F1: carboxyltransferase component (PccB), I3R7F2: essential small subunit PccX
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Subunits

Subunits Comment Organism
More the enzyme consists of a fusion protein of a biotin carboxylase and a biotin-carboxyl carrier protein (PccA, HFX_2490), a carboxyltransferase component (PccB, HFX_2478), and an essential small subunit (PccX, HFX_2479) Haloferax mediterranei

Synonyms

Synonyms Comment Organism
PCC
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 Haloferax mediterranei

General Information

General Information Comment Organism
malfunction gene knockout/complementation demonstrates that the enzyme consists of a fusion protein of a biotin carboxylase and a biotin-carboxyl carrier protein (PccA, HFX_2490), a carboxyltransferase component (PccB, HFX_2478), and an essential small subunit (PccX, HFX_2479). Knockout of pccBX leads to an inability to utilize propionate and a higher intracellular propionyl-CoA level, indicating that the enzyme is indispensable for propionyl-CoA utilization. the pccBX-deleted strain displays multiple phenotypic changes, including retarded cell growth, decreased glucose consumption, impaired PHBV biosynthesis, and wrinkled cells. Genome-wide microarray analysis shows that many genes for glycolysis, pyruvate oxidation, PHBV accumulation, electron transport, and stress responses are affected in the pccBX-deleted strain Haloferax mediterranei
metabolism the enzyme is indispensability for propionyl-CoA assimilation und the global metabolism of Haloferax mediterranei Haloferax mediterranei