Structure and reactivity in the non-mevalonate pathway of isoprenoid biosynthesis

2003 ◽  
Vol 31 (3) ◽  
pp. 537-542 ◽  
Author(s):  
W.N. Hunter ◽  
C.S. Bond ◽  
M. Gabrielsen ◽  
L.E. Kemp
Keyword(s):  
Escherichia Coli ◽  
Secondary Structure ◽  
Drug Targets ◽  
Active Sites ◽  
Quaternary Structure ◽  
Mevalonate Pathway ◽  
Isoprenoid Biosynthesis ◽  
Microbial Pathogens ◽  
Function Structure ◽  
Microbial Agents

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.

Physical studies on the ribosomal "A" protein from two archaebacteria, Halobacterium cutirubrum and Methanobacterium thermoautotrophicum

1984 ◽  
Vol 62 (1) ◽  
pp. 44-48 ◽  
Author(s):  
A. T. Gudkov ◽  
S. Yu Venyaminov ◽  
A. T. Matheson
Keyword(s):  
Escherichia Coli ◽  
Circular Dichroism ◽  
Secondary Structure ◽  
Quaternary Structure ◽  
Methanobacterium Thermoautotrophicum ◽  
Sedimentation Equilibrium ◽  
Effect Of Temperature ◽  
Extreme Halophile ◽  
Moderate Halophile ◽  
Circular Dichroïsm

Physical studies on the effect of temperature and ionic conditions on the secondary, tertiary, and quaternary structure of the ribosomal "A" protein, equivalent to L7/L12 in Escherichia coli, from two archaebacteria were performed using circular dichroism and sedimentation equilibrium measurements. The two archaebacteria investigated were Halobacterium cutirubrum, an extreme halophile, and Methanobacterium thermoautotrophicum, a thermophile which also showed properties of a moderate halophile. The changes in the secondary structure and the thermostability of these proteins were directly related to the internal salt concentrations of the two archaebacteria. At the higher salt concentrations the changes in the secondary structure resulted in changes in the tertiary and quaternary structure of these proteins.

Properties and inhibition of the first two enzymes of the non-mevalonate pathway of isoprenoid biosynthesis

2000 ◽  
Vol 28 (6) ◽  
pp. 792-793 ◽  
Author(s):  
C. Mueller ◽  
J. Schwender ◽  
J. Zeidler ◽  
H. K. Lichtenthaler
Keyword(s):  
Escherichia Coli ◽  
Mevalonate Pathway ◽  
Isoprenoid Biosynthesis ◽  
Mep Pathway ◽  
Ph Optimum ◽  
Antibacterial Drugs ◽  
Chloroplast Stroma

Enzymes of the 1-deoxy-D-xylulose 5-phosphate/2-C-methylerythritol 4-phosphate (DOXP/MEP) pathway are targets for new herbicides and antibacterial drugs. Until now, no inhibitors for the DOXP synthase have been known of. We show that one of the breakdown products of the herbicide clomazone affects the DOXP synthase. One inhibitor of the non-mevalonate pathway, fosmidomycin, blocks the DOXP reductoisomerase (DXR) of plants and bacteria. The I50 values of plants are, however, higher than those found for the DXR of Escherichia coli. The DXR of plants, isolated from barley seedlings, shows a pH optimum of 8.1, which is typical for enzymes active in the chloroplast stroma.

scholarly journals GcpE Is Involved in the 2-C-Methyl-d-Erythritol 4-Phosphate Pathway of Isoprenoid Biosynthesis in Escherichia coli

2001 ◽  
Vol 183 (8) ◽  
pp. 2411-2416 ◽  
Author(s):  
Boran Altincicek ◽  
Ann-Kristin Kollas ◽  
Silke Sanderbrand ◽  
Jochen Wiesner ◽  
Martin Hintz ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Mevalonate Pathway ◽  
Genetically Engineered ◽  
Isoprenoid Biosynthesis ◽  
Mep Pathway ◽  
E Coli

ABSTRACT In a variety of organisms, including plants and several eubacteria, isoprenoids are synthesized by the mevalonate-independent 2-C-methyl-d-erythritol 4-phosphate (MEP) pathway. Although different enzymes of this pathway have been described, the terminal biosynthetic steps of the MEP pathway have not been fully elucidated. In this work, we demonstrate that thegcpE gene of Escherichia coli is involved in this pathway. E. coli cells were genetically engineered to utilize exogenously provided mevalonate for isoprenoid biosynthesis by the mevalonate pathway. These cells were then deleted for the essential gcpE gene and were viable only if the medium was supplemented with mevalonate or the cells were complemented with an episomal copy of gcpE.

Characterization of Tamm-Horsfall Urinary Glycoprotein

1973 ◽  
Vol 31 ◽  
pp. 420-421
Author(s):  
John P. Robinson ◽  
J. David Puett
Keyword(s):  
Electron Microscopy ◽  
Circular Dichroism ◽  
Secondary Structure ◽  
Quaternary Structure ◽  
Normal Adult ◽  
Morphological Properties ◽  
Adult Males ◽  
Circular Dichroïsm ◽  
Urinary Glycoprotein

Much work has been reported on the chemical, physical and morphological properties of urinary Tamm-Horsfall glycoprotein (THG). Although it was once reported that cystic fibrotic (CF) individuals had a defective THG, more recent data indicate that THG and CF-THG are similar if not identical.No studies on the conformational aspects have been reported on this glycoprotein using circular dichroism (CD). We examined the secondary structure of THG and derivatives under various conditions and have correlated these results with quaternary structure using electron microscopy.THG was prepared from normal adult males and CF-THG from a 16-year old CF female by the method of Tamm and Horsfall. CF female by the method of Tamm and Horsfall.

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