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Literature summary for 4.1.2.13 extracted from

  • Doyle, S.A.; Tolan, D.R.
    Characterization of recombinant human aldolase B and purification by metal chelate chromatography (1995), Biochem. Biophys. Res. Commun., 206, 902-908.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0016
-
D-fructose 1,6-bisphosphate liver enzyme, Homo sapiens
0.0035
-
D-fructose 1,6-bisphosphate recombinant enzyme Homo sapiens
1.1
-
fructose 1-phosphate recombinant enzyme Homo sapiens
2.3
-
fructose 1-phosphate liver enzyme Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
38000
-
4 * 38000, recombinant aldolase A and liver enzyme, SDS-PAGE Homo sapiens
120000
-
liver enzyme, gel filtration Homo sapiens
170000
-
recombinant aldolase B, gel filtration Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant aldolase B and liver enzyme Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-fructose 1,6-bisphosphate
-
Homo sapiens glycerone phosphate + D-glyceraldehyde 3-phosphate
-
?

Subunits

Subunits Comment Organism
tetramer 4 * 38000, recombinant aldolase A and liver enzyme, SDS-PAGE Homo sapiens