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Literature summary for 2.1.1.222 extracted from

  • Xing, L.; Zhu, Y.; Fang, P.; Wang, J.; Zeng, F.; Li, X.; Teng, M.; Li, X.
    Crystallization and preliminary crystallographic studies of UbiG, an O-methyltransferase from Escherichia coli (2011), Acta Crystallogr. Sect. F, 67, 727-729.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapor diffusion method, using 0.1 M HEPES pH 7.5 and 20% (w/v) polyethylene glycol 10000 or 10% (v/v) 2-methyl-2,4-pentanediol and 0.1 M HEPES pH 7.0 Escherichia coli

Protein Variants

Protein Variants Comment Organism
L132Q the mutation results in ubiquinone deficiency in Escherichia coli leading to a high sensitivity to thiols and a failure to grow on succinate Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
26600
-
 x * 26600, SDS-PAGE Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA column chromatography, Superdex 200 gel filtration, and DEAE anion-exchange chromatography Escherichia coli

Subunits

Subunits Comment Organism
? x * 26600, SDS-PAGE Escherichia coli

Synonyms

Synonyms Comment Organism
UbiG
-
 Escherichia coli

General Information

General Information Comment Organism
metabolism the enzyme is required for both O-methylation steps in ubiquinone biosynthesis Escherichia coli