Tutorial:Basic Chemistry Topics: Difference between revisions
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The summary of the research artical will be confusing, you are not expected to understand it completely to benefit from the tutorial. The reasearch artical is used as a refrence to demonstrate the chemistry topics we will be discussing. | The summary of the research artical will be confusing, you are not expected to understand it completely to benefit from the tutorial. The reasearch artical is used as a refrence to demonstrate the chemistry topics we will be discussing. | ||
'''==Summary: Scientific Research Artical==''' | |||
The study where this molecule was obtained is named "Aminoglycoside 2'-N-acetyltransferase from Mycobacterium tuberculosis-Complex with Coenzyme A and Tobramycin". The study focused on AAC (2’)- Ic also known as aminoglycoside 2’- N- acetyltransferase. The scientist’s in the study determined the crystal structure of AAC (2’)-Ic from Mycobacterium tuberculosis. The specific fold of AAC (2’)-Ic places in the GNAT or GCN5-related N-acetyltransferase superfamily. Although the physiological function of AAC(2’)-Ic in not certain, the crystal structure they determined allowed them to hypothesize. Through the crystal structure they determined that this enzyme might acetylate mycothiol. Mycothiol is key biosynthetic intermediate and the major reducing agent in mycobacterium. This enzyme is capable of acetylating aminoglycosides bearing a 2’ amino group, when this occurs the aminoglycoside antibiotic becomes inactive. | The study where this molecule was obtained is named "Aminoglycoside 2'-N-acetyltransferase from Mycobacterium tuberculosis-Complex with Coenzyme A and Tobramycin". The study focused on AAC (2’)- Ic also known as aminoglycoside 2’- N- acetyltransferase. The scientist’s in the study determined the crystal structure of AAC (2’)-Ic from Mycobacterium tuberculosis. The specific fold of AAC (2’)-Ic places in the GNAT or GCN5-related N-acetyltransferase superfamily. Although the physiological function of AAC(2’)-Ic in not certain, the crystal structure they determined allowed them to hypothesize. Through the crystal structure they determined that this enzyme might acetylate mycothiol. Mycothiol is key biosynthetic intermediate and the major reducing agent in mycobacterium. This enzyme is capable of acetylating aminoglycosides bearing a 2’ amino group, when this occurs the aminoglycoside antibiotic becomes inactive. | ||
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__TOC__ | __TOC__ | ||
''' | =='''Objectives'''== | ||
By the end of this tutorial you should be able to: | By the end of this tutorial you should be able to: | ||