PF22613

Transketolase-like TK C-terminal domain

Pfam entry
Member databasePfam
Pfam typedomain
Short nameTransketolase_C_1
ClanTKC_like
Author Bateman A;0000-0002-6982-4660 Chuguransky S;0000-0002-0520-0736
Sequence Ontology0000417

Description

This entry represents the C-terminal domain found in transketolase and transketolase-like enzymes [1-5], such as pyruvate dehydrogenase E1 component (OPD1)
[1]
.

References

1.Structure of the pyruvate dehydrogenase multienzyme complex E1 component from Escherichia coli at 1.85 A resolution. Arjunan P, Nemeria N, Brunskill A, Chandrasekhar K, Sax M, Yan Y, Jordan F, Guest JR, Furey W. Biochemistry 41, 5213-21, (2002). View articlePMID: 11955070

Further reading

2. Identification of catalytically important residues in yeast transketolase. Wikner C, Nilsson U, Meshalkina L, Udekwu C, Lindqvist Y, Schneider G. Biochemistry 36, 15643-9, (1997). View articlePMID: 9398292

3. Transketolase from Leishmania mexicana has a dual subcellular localization. Veitch NJ, Maugeri DA, Cazzulo JJ, Lindqvist Y, Barrett MP. Biochem. J. 382, 759-67, (2004). View articlePMID: 15149284

4. Structure and properties of an engineered transketolase from maize. Gerhardt S, Echt S, Busch M, Freigang J, Auerbach G, Bader G, Martin WF, Bacher A, Huber R, Fischer M. Plant Physiol. 132, 1941-9, (2003). View articlePMID: 12913150

5. Snapshot of a key intermediate in enzymatic thiamin catalysis: crystal structure of the alpha-carbanion of (alpha,beta-dihydroxyethyl)-thiamin diphosphate in the active site of transketolase from Saccharomyces cerevisiae. Fiedler E, Thorell S, Sandalova T, Golbik R, Konig S, Schneider G. Proc. Natl. Acad. Sci. U.S.A. 99, 591-5, (2002). View articlePMID: 11773632

This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice and Terms of Use.