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Literature summary extracted from

  • Rellos, P.; Sygusch, J.; Cox, T.M.
    Expression, purification, and characterization of natural mutants of human aldolase B. Role of quaternary structure in catalysis (2000), J. Biol. Chem., 275, 1145-1151.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.2.13 expressed in Escherichia coli Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
4.1.2.13 A149P tetramers dissociate into subunits with greatly impaired enzymatic activity Homo sapiens
4.1.2.13 A174D tetramers dissociate into subunits with greatly impaired enzymatic activity, extremely labile mutant, aggregates rapidly Homo sapiens
4.1.2.13 A337V retained tetrameric structure, altered kinetic properties Homo sapiens
4.1.2.13 L256P tetramers dissociate into subunits with greatly impaired enzymatic activity Homo sapiens
4.1.2.13 N334K tetramers dissociate into subunits with greatly impaired enzymatic activity Homo sapiens
4.1.2.13 R303W retained tetrameric structure, altered kinetic properties Homo sapiens
4.1.2.13 W147R retained tetrameric structure, altered kinetic properties Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.2.13 0.0024
-
 D-Fructose 1-phosphate wild-type, 22°C, pH 7.6 Homo sapiens
4.1.2.13 0.0033
-
 D-Fructose 1-phosphate L256P, 22°C, pH 7.6 Homo sapiens
4.1.2.13 0.004
-
 D-fructose 1,6-bisphosphate wild-type, 22°C, pH 7.6 Homo sapiens
4.1.2.13 0.0059
-
 D-fructose 1,6-bisphosphate L256P, 22°C, pH 7.6 Homo sapiens
4.1.2.13 0.0098
-
 D-Fructose 1-phosphate A149P, 22°C, pH 7.6 Homo sapiens
4.1.2.13 0.022
-
 D-fructose 1,6-bisphosphate A337V, 22°C, pH 7.6 Homo sapiens
4.1.2.13 0.024
-
 D-Fructose 1-phosphate A337V, 22°C, pH 7.6 Homo sapiens
4.1.2.13 0.0266
-
 D-Fructose 1-phosphate W147R, 22°C, pH 7.6 Homo sapiens
4.1.2.13 0.027
-
 D-fructose 1,6-bisphosphate A149P, 22°C, pH 7.6 Homo sapiens
4.1.2.13 0.047
-
 D-fructose 1,6-bisphosphate W147R, 22°C, pH 7.6 Homo sapiens
4.1.2.13 0.33
-
 D-fructose 1,6-bisphosphate R303W, 22°C, pH 7.6 Homo sapiens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.2.13 additional information
-
 L256P mutant exists as tetramer partly dissociated into its subunits, A149P and N334K exist as mixture of protein conformers that encompass all molecular sizes between tetramer and monomer Homo sapiens
4.1.2.13 40000 60000 gel filtration, monomeric form, A149P, N334K, L256P, A337V mutant Homo sapiens
4.1.2.13 158000
-
 gel filtration, W147R, R303W, A337V mutant Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.2.13 D-fructose 1,6-bisphosphate Homo sapiens
-
 glycerone phosphate + D-glyceraldehyde 3-phosphate
-
 r

Organism

EC Number Organism UniProt Comment Textmining
4.1.2.13 Homo sapiens
-
 patients with fructose intolerance
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.2.13 homogeneity Homo sapiens

Storage Stability

EC Number Storage Stability Organism
4.1.2.13 wild-type enzyme: 50% loss of activity after 3 months, mutants: accelerated loss of activity Homo sapiens

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
4.1.2.13 dimer A149P and N334K mutants exist as mixture of protein conformers that encompass all molecular sizes between tetramer and monomer Homo sapiens
4.1.2.13 monomer A149P and N334K mutants exist as mixture of protein conformers that encompass all molecular sizes between tetramer and monomer Homo sapiens
4.1.2.13 tetramer L256P mutant exists as tetramer partly dissociated into its subunits, A149P and N334K exist as mixture of protein conformers that encompass all molecular sizes between tetramer and monomer Homo sapiens
4.1.2.13 trimer A149P and N334K mutants exist as mixture of protein conformers that encompass all molecular sizes between tetramer and monomer Homo sapiens