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Literature summary for 4.1.2.13 extracted from

  • St-Jean, M.; Blonski, C.; Sygusch, J.
    Charge stabilization and entropy reduction of central lysine residues in fructose-bisphosphate aldolase (2009), Biochemistry, 48, 4528-4537.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21 SI cells Oryctolagus cuniculus

Crystallization (Commentary)

Crystallization (Comment) Organism
D33N and D33S mutant enzymes Oryctolagus cuniculus

Protein Variants

Protein Variants Comment Organism
D33N the mutation drastically reduces the rate of turnover but does not impact substrate binding Oryctolagus cuniculus
D33S the mutation drastically reduces the rate of turnover but does not impact substrate binding Oryctolagus cuniculus
E187A the mutation drastically reduces the rate of turnover Oryctolagus cuniculus
E187Q the mutation drastically reduces the rate of turnover Oryctolagus cuniculus
K107M the mutation drastically reduces the rate of turnover Oryctolagus cuniculus
K146A the mutation drastically reduces the rate of turnover Oryctolagus cuniculus
K146M the mutation drastically reduces the rate of turnover Oryctolagus cuniculus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0042
-
D-fructose 1,6-bisphosphate mutant enzyme D33N Oryctolagus cuniculus
0.0051
-
D-fructose 1,6-bisphosphate native wild type enzyme Oryctolagus cuniculus
0.0061
-
D-fructose 1,6-bisphosphate mutant enzyme E187A Oryctolagus cuniculus
0.0084
-
D-fructose 1,6-bisphosphate mutant enzyme D33S Oryctolagus cuniculus
0.0134
-
D-fructose 1,6-bisphosphate mutant enzyme E187Q Oryctolagus cuniculus
0.0204
-
D-fructose 1,6-bisphosphate mutant enzyme K146M Oryctolagus cuniculus
0.0412
-
D-fructose 1,6-bisphosphate mutant enzyme K107M Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus P00883
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Oryctolagus cuniculus

Source Tissue

Source Tissue Comment Organism Textmining
muscle
-
Oryctolagus cuniculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-fructose 1,6-bisphosphate
-
Oryctolagus cuniculus glycerone phosphate + D-glyceraldehyde 3-phosphate
-
r

Synonyms

Synonyms Comment Organism
FBP aldolase
-
Oryctolagus cuniculus
fructose-1,6-bisphosphate muscle aldolase
-
Oryctolagus cuniculus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0002
-
D-fructose 1,6-bisphosphate turnover number less than 0.0002 sec-1, mutant enzyme K146A Oryctolagus cuniculus
0.0019
-
D-fructose 1,6-bisphosphate mutant enzyme K146M Oryctolagus cuniculus
0.002
-
D-fructose 1,6-bisphosphate mutant enzyme D33S Oryctolagus cuniculus
0.003
-
D-fructose 1,6-bisphosphate mutant enzyme D33N Oryctolagus cuniculus
0.005
-
D-fructose 1,6-bisphosphate mutant enzyme E187Q Oryctolagus cuniculus
0.046
-
D-fructose 1,6-bisphosphate mutant enzyme E187A Oryctolagus cuniculus
0.65
-
D-fructose 1,6-bisphosphate mutant enzyme K107M Oryctolagus cuniculus
13.22
-
D-fructose 1,6-bisphosphate native wild type enzyme Oryctolagus cuniculus