Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Publication

Aspartate 155 of human transketolase is essential for thiamine diphosphate-magnesium binding, and cofactor binding is required for dimer formation.

Wang JJ, Martin PR, Singleton CK

Active human transketolase is a homodimeric enzyme possessing two active sites, each with a non-covalently bound thiamine diphosphate and magnesium. Both subunits contribute residues at each site which are involved in cofactor binding and in catalysis. His-tagged transketolase, produced in E. coli, was similar to transketolase purified from human tissues with respect to Km apps for cofactor and substrates and ... [more]

Biochim. Biophys. Acta Sep. 05, 1997; 1341(2);165-72 [Pubmed: 9357955]

Throughput

  • Low Throughput

Curated By

  • BioGRID