Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.1.1.222 extracted from

  • Zhu, Y.; Jiang, X.; Wang, C.; Liu, Y.; Fan, X.; Zhang, L.; Niu, L.; Teng, M.; Li, X.
    Structural insights into the methyl donor recognition model of a novel membrane-binding protein UbiG (2016), Sci. Rep., 6, 23147 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.1.1.222

Crystallization (Commentary)

Crystallization (Comment) Organism
structure of UbiGDELTA165-187 in complex with SAH Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information for mutant UbiGDELTA 165-187 lacking the sequence insertion that covers the methyl donor binding pocket, the binding affinity to SAH is approximately 58fold higher than that of wild-type Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane the membrane-binding region of UbiG gates the entrance of methyl donor Escherichia coli 16020
-

Organism

Organism UniProt Comment Textmining
Escherichia coli C3T302
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + 3-(all-trans-polyprenyl)benzene-1,2-diol
-
 Escherichia coli S-adenosyl-L-homocysteine + 2-methoxy-6-(all-trans-polyprenyl)phenol
-
 ?

Synonyms

Synonyms Comment Organism
UbiG
-
 Escherichia coli
ubiquinone biosynthesis O-methyltransferase
-
 Escherichia coli

General Information

General Information Comment Organism
physiological function the membrane-binding region of UbiG gates the entrance of methyl donor. When bound with liposome, UbiG displays an enhanced binding ability toward the methyl donor product S-adenosylhomocysteine Escherichia coli