نتایج جستجو برای: Pantothenate synthetase (PanC)

تعداد نتایج: 17708  

Mycobacterium tuberculosis, the main cause of tuberculosis (TB), has still remained a global health crisis especially in developing countries. Tuberculosis treatment is a laborious and lengthy process with high risk of non compliance, cytotoxicity adverse events and drug resistance in patient. Recently, there has been an alarming rise of drug resistant in TB. In this regard, it is an unmet need...

Mycobacterium tuberculosis, the main cause of tuberculosis (TB), has still remained a global health crisis especially in developing countries. Tuberculosis treatment is a laborious and lengthy process with high risk of non compliance, cytotoxicity adverse events and drug resistance in patient. Recently, there has been an alarming rise of drug resistant in TB. In this regard, it is an unmet need...

Journal: :iranian journal of pharmaceutical research 0
baharak khoshkholgh-sima department of biology, science and research branch, islamic azad university, tehran, iran soroush sardari drug design and bioinformatics unit, medical biotechnology department, biotechnology research center, pasteur institute, #69, pasteur ave., tehran, 13164, iran. jalal izadi mobarakeh physiology and pharmacology department, pasteur institute of iran, #69, pasteur ave., tehran, 13164, iran ramezan ali khavari-nejad department of biology, science and research branch, islamic azad university, tehran, iran.

mycobacterium tuberculosis, the main cause of tuberculosis (tb), has still remained a global health crisis especially in developing countries. tuberculosis treatment is a laborious and lengthy process with high risk of non compliance, cytotoxicity adverse events and drug resistance in patient. recently, there has been an alarming rise of drug resistant in tb. in this regard, it is an unmet need...

Journal: :Biochemistry 2001
R Zheng J S Blanchard

Pantothenate synthetase (EC 6.3.2.1), encoded by the panC gene, catalyzes the essential ATP-dependent condensation of D-pantoate and beta-alanine to form pantothenate in bacteria, yeast and plants. Pantothenate synthetase from Mycobacterium tuberculosis was expressed in E. coli, purified to homogeneity, and found to be a homodimer with a subunit molecular mass of 33 kDa. Initial velocity, produ...

2015
Baharak Khoshkholgh-Sima Soroush Sardari Jalal Izadi Mobarakeh Ramezan Ali Khavari-Nejad

Mycobacterium tuberculosis, the main cause of tuberculosis (TB), has still remained a global health crisis especially in developing countries. Tuberculosis treatment is a laborious and lengthy process with high risk of noncompliance, cytotoxicity adverse events and drug resistance in patient. Recently, there has been an alarming rise of drug resistant in TB. In this regard, it is an unmet need ...

2013
Anuradha Kumar Allen Casey Joshua Odingo Edward A. Kesicki Garth Abrahams Michal Vieth Thierry Masquelin Valerie Mizrahi Philip A. Hipskind David R. Sherman Tanya Parish

The enzyme pantothenate synthetase, PanC, is an attractive drug target in Mycobacterium tuberculosis. It is essential for the in vitro growth of M. tuberculosis and for survival of the bacteria in the mouse model of infection. PanC is absent from mammals. We developed an enzyme-based assay to identify inhibitors of PanC, optimized it for high-throughput screening, and tested a large and diverse...

Journal: :Applied and environmental microbiology 1999
H Sahm L Eggeling

D-Pantothenate is synthesized via four enzymes from ketoisovalerate, which is an intermediate of branched-chain amino acid synthesis. We quantified three of these enzyme activities in Corynebacterium glutamicum and determined specific activities ranging from 0.00014 to 0.001 micromol/min mg (protein)-1. The genes encoding the ketopantoatehydroxymethyl transferase and the pantothenate synthetase...

Journal: :Journal of bacteriology 1985
D S Vallari C O Rock

Mutants of Escherichia coli K-12 defective in the pantothenate permease (panF) were isolated and characterized. The panF mutation resulted in the complete loss of pantothenate uptake and of the ability to use extracellular vitamin for growth. The growth phenotypes of panF panD, panF panB, and panF panC double mutants showed that the cytoplasmic membrane was impermeable to external pantothenate....

Journal: :The Biochemical journal 1999
U Genschel C A Powell C Abell A G Smith

We have isolated a Lotus japonicus cDNA for pantothenate (vitamin B(5)) synthetase (PS) by functional complementation of an Escherichia coli panC mutant (AT1371). A rice (Oryza sativum) expressed sequence tag, identified by sequence similarity to PS, was also able to complement the E. coli auxotroph, as was an open reading frame from Saccharomyces cerevisiae (baker's yeast). The Lotus and rice ...

Journal: :Biochemistry 2003
LaKenya Williams Renjian Zheng John S Blanchard Frank M Raushel

Pantothenate synthetase from Mycobacterium tuberculosis catalyzes the formation of pantothenate from ATP, D-pantoate, and beta-alanine. The formation of a kinetically competent pantoyl-adenylate intermediate was established by the observation of a positional isotope exchange (PIX) reaction within (18)O-labeled ATP in the presence of d-pantoate. When [betagamma-(18)O(6)]-ATP was incubated with p...

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