Bacteria have a rich collection of biochemical pathways for the synthesis of complex metabolites. These conversions often involve chemical reactions that are hard to reproduce in the laboratory. An area of considerable interest is in the manipulation and synthesis of carbohydrates. In contrast with amino acids, carbohydrates are densely functionalized (each carbon atom is attached to at least one heteroatom) and this holds out the prospect of discovering novel enzyme mechanisms. The results from the study of the biosynthetic dTDP-l-rhamnose pathway are discussed. dTDP-l-rhamnose is a key intermediate in many pathogenic bacteria, as it is the donor for l-rhamnose, which is found in the cell wall of important human pathogens, such as Mycobacteria tuberculosis and Salmonella typhimurium. All four enzymes have been structurally characterized; in particular, the acquisition of structural data on substrate complexes was extremely useful. The structural data have guided site-directed-mutagenesis studies that have been used to test mechanistic hypotheses. The results shed light on three classes of enzyme mechanism: nucleotide condensation, short-chain dehydrogenase activity and epimerization.
Skip Nav Destination
Article navigation
Conference Article|
June 01 2003
A structural perspective on the enzymes that convert dTDP-d-glucose into dTDP-l-rhamnose
C. Dong;
C. Dong
1
*Centre for Biomolecular Science, The University, St. Andrews KY16 9ST, U.K.
Search for other works by this author on:
K. Beis;
K. Beis
1
*Centre for Biomolecular Science, The University, St. Andrews KY16 9ST, U.K.
Search for other works by this author on:
M.-F. Giraud;
M.-F. Giraud
1
†Institut de Biochemie et de Génétique Cellulaires du CNRS, Université Victor Segalen, Bordeaux 2, 1 rue Camille Saint-Saëns, F-33 077 Bordeaux cedex, France
Search for other works by this author on:
W. Blankenfeldt;
W. Blankenfeldt
1
‡Max-Planck-Institute of Molecular Physiology, Otto-Hahn-Str. 11, 44227 Dortmund, Germany
Search for other works by this author on:
S. Allard;
S. Allard
1
§Department of Biochemistry, University of Wisconsin – Madison, Madison, WI 53705, U.S.A.
Search for other works by this author on:
L.L. Major;
L.L. Major
1
*Centre for Biomolecular Science, The University, St. Andrews KY16 9ST, U.K.
Search for other works by this author on:
I.D. Kerr;
I.D. Kerr
1
*Centre for Biomolecular Science, The University, St. Andrews KY16 9ST, U.K.
Search for other works by this author on:
C. Whitfield;
C. Whitfield
∥Department of Microbiology, University of Guelph, Guelph, Canada N1G 2W1
Search for other works by this author on:
J.H. Naismith
J.H. Naismith
2
*Centre for Biomolecular Science, The University, St. Andrews KY16 9ST, U.K.
2To whom correspondence should be addressed (e-mail naismith@st-and.ac.uk).
Search for other works by this author on:
Publisher: Portland Press Ltd
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2003 Biochemical Society
2003
Biochem Soc Trans (2003) 31 (3): 532–536.
Citation
C. Dong, K. Beis, M.-F. Giraud, W. Blankenfeldt, S. Allard, L.L. Major, I.D. Kerr, C. Whitfield, J.H. Naismith; A structural perspective on the enzymes that convert dTDP-d-glucose into dTDP-l-rhamnose. Biochem Soc Trans 1 June 2003; 31 (3): 532–536. doi: https://doi.org/10.1042/bst0310532
Download citation file:
Sign in
Don't already have an account? Register
Sign in to your personal account
You could not be signed in. Please check your email address / username and password and try again.
Captcha Validation Error. Please try again.