Is transketolase-like protein, TKTL1, transketolase?
| Autor: | Olga N. Solovjeva, L. E. Meshalkina, O. N. Koroleva, Drutsa Vl, German A. Kochetov |
|---|---|
| Rok vydání: | 2013 |
| Předmět: |
Site-specific mutagenesis
Mutant Mutagenesis (molecular biology technique) TKTL1 Transketolase Biology Humans Site-directed mutagenesis Molecular Biology chemistry.chemical_classification Wild type Molecular biology Recombinant Proteins Amino acid Transketolase-like protein 1 Kinetics Biochemistry chemistry Oncology Mutation Mutagenesis Site-Directed Transketolase activity Thiamine diphosphate Molecular Medicine Electrophoresis Polyacrylamide Gel Mutant Proteins Thiamine Thiamine Pyrophosphate Human transketolase |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1832(3):387-390 |
| ISSN: | 0925-4439 |
| DOI: | 10.1016/j.bbadis.2012.12.004 |
| Popis: | Until recently it was assumed that the transketolase-like protein (TKTL1) detected in the tumor tissue, is catalytically active mutant form of human transketolase (hTKT). Human TKT shares 61% sequence identity with TKTL1. And the two proteins are 77% homologous at the amino acid level. The major difference is the absence of 38 amino acid residues in the N-terminal region of TKTL1. Site-specific mutagenesis was used for modifying hTKT gene; the resulting construct had a 114-bp deletion corresponding to a deletion of 38 amino acid residues in hTKT protein. Wild type hTKT and mutant variant (DhTKT) were expressed in Escherichia coli and isolated using Ni-agarose affinity chromatography. We have demonstrated here that DhTKT is devoid of transketolase activity and lacks bound thiamine diphosphate (ThDP). In view of these results, it is unlikely that TKTL1 may be a ThDP-dependent protein capable of catalyzing the transketolase reaction, as hypothesized previously. |
| Databáze: | OpenAIRE |
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