Transketolase, C-terminal domain

Definition

The C-terminal domain of transketolase has been proposed as a regulatory molecule binding site [[cite:PMID:8176731], [cite:PMID:1628611]]. Transketolase [ec:2.2.1.1] (TK) catalyses the reversible transfer of a two-carbon ketol unit from xylulose 5-phosphate to an aldose receptor, such as ribose 5-phosphate, to form sedoheptulose 7-phosphate and glyceraldehyde 3- phosphate. This enzyme, together with transaldolase, provides a link between the glycolytic and pentose-phosphate pathways. TK requires thiamine pyrophosphate as a cofactor. In most sources where TK has been purified, it is a homodimer of approximately 70kDa subunits. TK sequences from a variety of eukaryotic and prokaryotic sources [[cite:PMID:1567394], [cite:PMID:1737042]] show that the enzyme has been evolutionarily conserved. In the peroxisomes of methylotrophic yeast Pichia angusta (Yeast) (Hansenula polymorpha), there is a highly related enzyme, dihydroxy-acetone synthase (DHAS) [ec:2.2.1.3] (also known as formaldehyde transketolase), which exhibits a very unusual specificity by including formaldehyde amongst its substrates.

5 human proteins with this domain

Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.

Download CSV (5 proteins: gene, accession, name)

• BCKDHB
• PDHB
• TKT
• TKTL1
• TKTL2