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Literature summary extracted from

  • Soh, Y.; Song, B.J.; Jeng, J.; Kallarakal, A.T.
    Critical role of Arg433 in rat transketolase activity as probed by site-directed mutagenesis (1998), Biochem. J., 333, 367-372.
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.2.1.1 expression in Escherichia coli Rattus norvegicus

Protein Variants

EC Number Protein Variants Comment Organism
2.2.1.1 R102A similar catalytyc activity like wild-type enzyme Rattus norvegicus
2.2.1.1 R350A lower activity than wild-type enzyme Rattus norvegicus
2.2.1.1 R433A lower activity than wild-type enzyme, less stable at 55°C than wild-type Rattus norvegicus
2.2.1.1 R506A lower activity than wild-type enzyme Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.2.1.1 0.0362
-
 D-ribose 5-phosphate wild-type Rattus norvegicus
2.2.1.1 0.0399
-
 D-xylulose 5-phosphate wild-type Rattus norvegicus
2.2.1.1 0.4579
-
 D-xylulose 5-phosphate R433A Rattus norvegicus
2.2.1.1 0.879
-
 D-ribose 5-phosphate R433A Rattus norvegicus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.2.1.1 74000
-
 alpha2 2 * 74000, SDS-PAGE Rattus norvegicus
2.2.1.1 148000
-
 PAGE Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
2.2.1.1 Rattus norvegicus
-
-
-

Subunits

EC Number Subunits Comment Organism
2.2.1.1 dimer alpha2 2 * 74000, SDS-PAGE Rattus norvegicus