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Literature summary extracted from

  • Choi, P.; Jo, J.; Lin, Y.; Lin, M.; Chou, C.; Dietrich, L.; Tong, L.
    A distinct holoenzyme organization for two-subunit pyruvate carboxylase (2016), Nat. Commun., 7, 12713 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.4.1.1
-
 Pseudomonas aeruginosa
6.4.1.1
-
 Methylobacillus flagellatus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.4.1.1 crystal structures of biotin carboxylase domain deletion mutant and of mutant K419A/E421A/E422A reveal an alpha2beta4 stoichiometry Methylobacillus flagellatus

Protein Variants

EC Number Protein Variants Comment Organism
6.4.1.1 A465R mutation in the alpha subunit, abolishes the formation of the holoenzyme, catalytically inactive Methylobacillus flagellatus
6.4.1.1 A55T mutation in the beta subunit, reduces activity by 50fold and interferes with biotin binding to the active site,mutant exhibits growth on pyruvate similar to the wild type Pseudomonas aeruginosa
6.4.1.1 D502A/E507A mutation in the alpha subunit, mutant forms a stable holoenzyme, about 40% of wild-type activity Methylobacillus flagellatus
6.4.1.1 H476A/E478A mutation in the alpha subunit, mutant forms a stable holoenzyme and is fully active Methylobacillus flagellatus
6.4.1.1 H476A/E478A/D502A/E507A mutation in the alpha subunit, abolishes the formation of the holoenzyme, catalytically inactive Methylobacillus flagellatus
6.4.1.1 K419A/E421A/E422A mutations bin the beta subunit designed to reduce the surface entropy. The mutations have no effect on the catalytic activity of the enzyme Methylobacillus flagellatus
6.4.1.1 K451stop mutation in alpha subunit, disrupts holoenzyme formation Pseudomonas aeruginosa
6.4.1.1 K572A mutation in the beta subunit, abolishes biotinylation and leads to growth defects in pyruvate that are similar to that of a gene deletion mutant Pseudomonas aeruginosa
6.4.1.1 Q452stop mutation in the alpha subunit, abolishes the formation of the holoenzyme Methylobacillus flagellatus
6.4.1.1 R401E mutation in the alpha subunit, mutant forms a stable holoenzyme, about 50% of wild-type activity Methylobacillus flagellatus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
6.4.1.1 340000
-
 analytical ultracentrifugation Methylobacillus flagellatus

Organism

EC Number Organism UniProt Comment Textmining
6.4.1.1 Methylobacillus flagellatus Q1H157
-
-
6.4.1.1 Methylobacillus flagellatus DSM 6875 Q1H157
-
-
6.4.1.1 Pseudomonas aeruginosa
-
-
-

Synonyms

EC Number Synonyms Comment Organism
6.4.1.1 Mfla_1512
-
 Methylobacillus flagellatus

General Information

EC Number General Information Comment Organism
6.4.1.1 physiological function a gene deletion mutant shows similar morphologies to those of the wild-typewhen succinate is supplied as the carbon source. When glucose or pyruvate is provided as the carbon source, the mutation prevents growth. In the colony morphology assay, the wild type initially produces a smooth colony, which forms wrinkle structures in the centre starting on day 3. The deletion mutant and K572A colonies begin to wrinkle on day 2 and exhibit a flatter morphology with several exaggerated wrinkles in a spoke formation Pseudomonas aeruginosa