scholarly journals Isoniazid induces expression of the antigen 85 complex in Mycobacterium tuberculosis.

1996 ◽  
Vol 40 (7) ◽  
pp. 1754-1756 ◽  
Author(s):  
T R Garbe ◽  
N S Hibler ◽  
V Deretic
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Antimicrobial Agents ◽  
Isonicotinic Acid ◽  
Acid Hydrazide ◽  
Isonicotinic Acid Hydrazide ◽  
Two Dimensional Gel Electrophoresis ◽  
Mycolic Acids ◽  
Mycobacterium Tuberculosis H37rv ◽  
Antigen 85 ◽  
Differential Gene

Exposure to isoniazid induced the expression of several secreted proteins in Mycobacterium tuberculosis H37Rv. Two-dimensional gel electrophoresis and immunoblot analyses indicated that two of the prominent isonicotinic acid hydrazide-inducible polypeptides were members of the antigen 85 complex, recently demonstrated to have mycolyltransferase activity. We postulate the existence of an intermediate, whose production is inhibited by isonicotinic acid hydrazide, which plays a negative feedback regulatory role in the metabolism of mycolic acids are revealed by the overexpression of the antigen 85 complex. The approach described here relies on analyses of differential gene expression following exposure to inhibitors and may become a more general tool in dissecting the effects of antimicrobial agents.

scholarly journals The purification and properties of peroxidase in Mycobacterium tuberculosis H37Rv and its possible role in the mechanism of action of isonicotinic acid hydrazide

1975 ◽  
Vol 149 (1) ◽  
pp. 187-197 ◽  
Author(s):  
B G Devi ◽  
M S Shaila ◽  
T Ramakrishnan ◽  
K P Gopinathan
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Thermal Inactivation ◽  
Isonicotinic Acid ◽  
Gel Filtration ◽  
Acid Hydrazide ◽  
Enzyme Reaction ◽  
Tuberculosis H37rv ◽  
Isonicotinic Acid Hydrazide ◽  
Mycobacterium Tuberculosis H37rv ◽  
Nad Glycohydrolase

Peroxidase from Mycobacterium tuberculosis H37Rv was purified to homogeneity. The homogeneous protein exhibits catalase and Y (Youatt's)-enzyme activities in addition to peroxidase activity. Further confirmation that the three activities are due to a single enzyme was accomplished by other criteria, such as differential thermal inactivation, sensitivity to different inhibitors, and co-purification. The Y enzyme (peroxidase) was separated from NADase (NAD+ glycohydrolase) inhibitor by gel filtration on Sephadex G-200. The molecular weights of peroxidase and NADase inhibitor, as determined by gel filtration, are 240000 and 98000 respectively. The Y enzyme shows two Km values for both isoniazid (isonicotinic acid hydrazide) and NAD at low and high concentrations. Analysis of the data by Hill plots revealed that the enzyme has one binding site at lower substrate concentrations and more than one at higher substrate concentration. The enzyme contains 6g-atoms of iron/mol. Highly purified preparations of peroxidases from different sources catalyse the Y-enzyme reaction, suggesting that the nature of the reaction may be a peroxidatic oxidation of isoniazid. Moreover, the Y-enzyme reaction is enhanced by O2. Isoniazid-resistant mutants do not exhibit Y-enzyme, peroxidase or catalase activities, and do not take up isoniazid. The Y-enzyme reaction is therefore implicated in the uptake of the drug.

ChemInform Abstract: New 1,4-Di-N-oxide-quinoxaline-2-ylmethylene Isonicotinic Acid Hydrazide Derivatives (VI) as anti-Mycobacterium tuberculosis Agents.

ChemInform ◽  
2011 ◽  
Vol 42 (45) ◽  
pp. no-no
Author(s):  
Enrique Torres ◽  
Elsa Moreno ◽  
Saioa Ancizu ◽  
Carlos Barea ◽  
Silvia Galiano ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Isonicotinic Acid ◽  
Acid Hydrazide ◽  
Isonicotinic Acid Hydrazide

scholarly journals New 1,4-di-N-oxide-quinoxaline-2-ylmethylene isonicotinic acid hydrazide derivatives as anti-Mycobacterium tuberculosis agents

2011 ◽  
Vol 21 (12) ◽  
pp. 3699-3703 ◽  
Author(s):  
Enrique Torres ◽  
Elsa Moreno ◽  
Saioa Ancizu ◽  
Carlos Barea ◽  
Silvia Galiano ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Isonicotinic Acid ◽  
Acid Hydrazide ◽  
Isonicotinic Acid Hydrazide

The Formation of 4-Pyridine Methanol from Isonicotinic Acid Hydrazide (Isoniazid) by Mycobacteria

1961 ◽  
Vol 14 (2) ◽  
pp. 308 ◽  
Author(s):  
J Youatt
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Infrared Spectra ◽  
Isonicotinic Acid ◽  
Acid Hydrazide ◽  
Isonicotinic Acid Hydrazide ◽  
Breakdown Product ◽  
Melting Points

4-Pyridine methanol has been isolated and identified as a breakdown product of isonicotinic acid hydrazide (isoniazid) by Mycobacterium tuberculosis B.C.G. The methiodide and hydrochloride mere prepared and analysed and mixed melting points were determined with synthetic 4-pyridine methanol derivatives. Ultraviolet and infrared spectra are shown.

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