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Literature summary for 4.1.2.13 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)

Cloned (Comment) Organism
expressed in Escherichia coli Homo sapiens

Protein Variants

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

KM Value [mM]

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

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
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
40000 60000 gel filtration, monomeric form, A149P, N334K, L256P, A337V mutant Homo sapiens
158000
-
gel filtration, W147R, R303W, A337V mutant Homo sapiens

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
patients with fructose intolerance
-

Purification (Commentary)

Purification (Comment) Organism
homogeneity Homo sapiens

Storage Stability

Storage Stability Organism
wild-type enzyme: 50% loss of activity after 3 months, mutants: accelerated loss of activity 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
-
r
D-Fructose 1-phosphate
-
Homo sapiens Glycerone phosphate + D-glyceraldehyde
-
?

Subunits

Subunits Comment Organism
dimer A149P and N334K mutants exist as mixture of protein conformers that encompass all molecular sizes between tetramer and monomer Homo sapiens
monomer A149P and N334K mutants exist as mixture of protein conformers that encompass all molecular sizes between tetramer and monomer Homo sapiens
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
trimer A149P and N334K mutants exist as mixture of protein conformers that encompass all molecular sizes between tetramer and monomer Homo sapiens