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Literature summary for 5.3.2.5 extracted from

  • Tamura, H.; Saito, Y.; Ashida, H.; Kai, Y.; Inoue, T.; Yokota, A.; Matsumura, H.
    Structure of the apo decarbamylated form of 2,3-diketo-5-methylthiopentyl-1-phosphate enolase from Bacillus subtilis (2009), Acta Crystallogr. Sect. D, 65, 942-951.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Escherichia coli Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
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-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from Escherichia coli Bacillus subtilis

Subunits

Subunits Comment Organism
dimer the active site is located at the open end of a C-terminal (beta/alpha)8-barrel, induced fit of Lys150 to the active site upon substrate binding Bacillus subtilis
More structure of the apo decarbamylated enzyme E form, computational structure analysis and modeling, structure comparison, overview. In the E form of DK-MTP-1P enolase the loop at 299-311, equivalent to loop-6 in RuBisCO, is in a closed conformation and the loop at 37-46, equivalent to the 60s loop, is positioned about 15 A away from the active site Bacillus subtilis

Synonyms

Synonyms Comment Organism
DKMTP-1P enolase
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Bacillus subtilis

General Information

General Information Comment Organism
physiological function 2,3-diketo-5-methylthiopentyl-1-phosphate enolase is a RuBisCO-like protein, that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate Bacillus subtilis