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Literature summary for 4.2.1.11 extracted from

  • Brewer, J.M.; Robson, R.L.; Glover, C.V.C.; Holland, M.J.; Lebioda, L.
    Preparation and characterization of the E168Q site-directed mutant of yeast enolase 1 (1993), Proteins Struct. Funct. Genet., 17, 426-434.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
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Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
E168Q the mutant has approximately 0.01% of the activity of native enolase. It binds 3-aminoenolpyruvate-2-phosphate, the 3-amino analogue of the product phosphoenolpyruvate and D-tartronate semialdehyde-2-phosphate, the aldehyde analogue of the substrate 2-phosphoglycerate, the latter two with affinities similar to those of the native enzyme Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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enolase 1 and mutant E168Q of enolase 1
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-phospho-D-glycerate
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Saccharomyces cerevisiae phosphoenolpyruvate
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