Cytosolic Enzymes in Peptidoglycan Biosynthesis as Potential Antibacterial Targets

1992 ◽  
pp. 176-204 ◽  
Author(s):  
W. Stephen Faraci
Keyword(s):  
Peptidoglycan Biosynthesis ◽  
Cytosolic Enzymes

Cytochemical Studies of Cell Wall Biosynthesis in Staphylococcus Aureus

1972 ◽  
Vol 30 ◽  
pp. 328-329
Author(s):  
Masaatsu Koike ◽  
Koichi Nakashima ◽  
Kyoko Iida
Keyword(s):  
Staphylococcus Aureus ◽  
Periodate Oxidation ◽  
Early Time ◽  
The Other ◽  
Penicillin G ◽  
Cell Wall Biosynthesis ◽  
Septal Wall ◽  
Peptidoglycan Biosynthesis ◽  
Gram Positive Bacteria ◽  
Cross Linkage

Penicillin exerts the activity to inhibit the peptide cross linkage between each polysaccharide backbone at the final stage of wall-peptidoglycan biosynthesis of bacteria. Morphologically, alterations of the septal wall and mesosome in gram-positive bacteria, which were occurred in early time after treatment with penicillin, have been observed. In this experiment, these alterations were cytochemically investigated by means of silver-methenamine staining after periodate oxidation, which is applied for detection of localization of wall mucopolysaccharide.Staphylococcus aureus strain 209P treated with 100 u/ml of penicillin G was divided into two aliquotes. One was fixed by Kellenberger-Ryter's OSO4 fixative at 30, 60 and 120 min after addition of the antibiotic, dehydrated through alcohol series, and embedded in Epon 812 (Specimen A). The other was fixed by 21 glutaraldehyde, dehydrated through glycolmethacrylate series and embedded in glycolmethacrylate mixture, according to Bernhard's method (Specimen B).

Ability of PknA, a mycobacterial eukaryotic-type serine/threonine kinase, to transphosphorylate MurD, a ligase involved in the process of peptidoglycan biosynthesis

2008 ◽  
Vol 415 (1) ◽  
pp. 27-33 ◽  
Author(s):  
Meghna Thakur ◽  
Pradip K. Chakraborti
Keyword(s):  
Protein Kinases ◽  
Solid Phase ◽  
Morphological Changes ◽  
Binding Assays ◽  
Serine Threonine Kinase ◽  
Threonine Kinase ◽  
Peptidoglycan Biosynthesis ◽  
Vitro Binding ◽  
Solid Phase Binding

Eukaryotic-type serine/threonine protein kinases in bacteria have been implicated in controlling a host of cellular activities. PknA is one of eleven such protein kinases from Mycobacterium tuberculosis which regulates morphological changes associated with cell division. In the present study we provide the evidence for the ability of PknA to transphosphorylate mMurD (mycobacterial UDP-N-acetylmuramoyl-L-alanine:D-glutamate-ligase), the enzyme involved in peptidoglycan biosynthesis. Its co-expression in Escherichia coli along with PknA resulted in phosphorylation of mMurD. Consistent with these observations, results of the solid-phase binding assays revealed a high-affinity in vitro binding between the two proteins. Furthermore, overexpression of m-murD in Mycobacterium smegmatis yielded a phosphorylated protein. The results of the present study therefore point towards the possibility of mMurD being a substrate of PknA.

A Phosphinate Inhibitor of themeso-Diaminopimelic Acid-Adding Enzyme (MurE) of Peptidoglycan Biosynthesis

1998 ◽  
Vol 63 (26) ◽  
pp. 10081-10085 ◽  
Author(s):  
Binqi Zeng ◽  
Kenny K. Wong ◽  
David L. Pompliano ◽  
Sreelatha Reddy ◽  
Martin E. Tanner
Keyword(s):  
Diaminopimelic Acid ◽  
Peptidoglycan Biosynthesis

Ethambutol targets the glutamate racemase of Mycobacterium tuberculosis—an enzyme involved in peptidoglycan biosynthesis

2018 ◽  
Vol 103 (2) ◽  
pp. 843-851 ◽  
Author(s):  
Alka Pawar ◽  
Prakash Jha ◽  
Chandrika Konwar ◽  
Uma Chaudhry ◽  
Madhu Chopra ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Peptidoglycan Biosynthesis ◽  
Glutamate Racemase

In vitro activation of 1,2-dichloroethane by microsomal and cytosolic enzymes

1980 ◽  
Vol 55 (2) ◽  
pp. 303-317 ◽  
Author(s):  
F.Peter Guengerich ◽  
W.Morgan Crawford ◽  
Jeanne Y. Domoradzki ◽  
Timothy L. Macdonald ◽  
Philip G. Watanabe
Keyword(s):  
In Vitro Activation ◽  
Cytosolic Enzymes
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