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

BRENDA support

Literature summary for 4.1.2.14 extracted from

  • Wymer, N.; Buchanan, L.V.; Henderson, D.; Mehta, N.; Botting, C.H.; Pocivavsek, L.; Fierke, C.A.; Toone, E.J.; Naismith, J.H.
    Directed evolution of a new catalytic site in 2-keto-3-deoxy-6-phosphogluconate aldolase from Escherichia coli (2001), Structure, 9, 1-9.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
-
Escherichia coli

Protein Variants

Protein Variants Comment Organism
K133Q no aldolase activity Escherichia coli
K133Q/T161K reduced catalytic efficiency Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
10
-
pyruvate pH 7.5, wild-type and K133Q/T161K mutant Escherichia coli
26.3
-
benzaldehyde pH 7.5, K133Q/T161K mutant Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A955
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxobutyrate + 2-pyridine carboxaldehyde weak substrate for wild-type enzyme, good substrate for K133Q/T161K mutant Escherichia coli ?
-
?
3-fluoropyruvate + 2-pyridine carboxaldehyde weak substrate for wild-type enzyme, good substrate for K133Q/T161K mutant Escherichia coli ?
-
?
pyruvate + benzaldehyde
-
Escherichia coli ?
-
?
pyruvate + D-erythrose weak substrate Escherichia coli ?
-
?
pyruvate + D-glyceraldehyde
-
Escherichia coli 2-dehydro-3-deoxy-D-gluconate
-
?

Subunits

Subunits Comment Organism
trimer crystallization experiments Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.000001
-
benzaldehyde pH 7.5, K133Q/T161K mutant Escherichia coli
0.0000046
-
pyruvate pH 7.5, K133Q/T161K mutant Escherichia coli
0.0121
-
pyruvate pH 7.5, wild-type Escherichia coli