Structure and reactivity in the non-mevalonate pathway of isoprenoid biosynthesis.
The function, structure and mechanism of two Escherichia coli enzymes involved in the non-mevalonate route of isoprenoid biosynthesis, 2C-methyl-D-erythritol 4-phosphate cytidylyltransferase and 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase, are reviewed. Comparisons of each with enzymes from microbial pathogens highlight important conservation of sequence suggestive of similarities in secondary structure, subunit folds, quaternary structure and active sites. Since both enzymes are validated drug targets, the models provide templates for structure-based design of anti-microbial agents targeting a number of serious human diseases.
Hunter
W N
WN
Division of Biological Chemistry and Molecular Microbiology, School of Life Sciences, University of Dundee, Dundee DD1 5EH, UK. w.n.hunter@dundee.ac.uk
Bond
C S
CS
Gabrielsen
M
M
Kemp
L E
LE
D000595:Amino Acid Sequence; D001665:Binding Sites; D004926:Escherichia coli / Q000201:enzymology*; D019476:Insect Proteins / Q000737:chemistry* / Q000378:metabolism*; D008798:Mevalonic Acid / Q000378:metabolism; D008958:Models, Molecular; D011487:Protein Conformation; D017368:Protein Prenylation / Q000502:physiology*; D016415:Sequence Alignment
D019476:Insect Proteins; C411804:MEP protein, 160 kDa, Tenebrio molitor; D008798:Mevalonic Acid