Tutorial:Basic Chemistry Topics: Difference between revisions
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=='''Summary: Scientific Research Artical'''== | =='''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 scientists in the study determined the crystal structure of AAC (2’)-Ic from Mycobacterium tuberculosis. The specific fold of AAC (2’)-Ic is placed in the GNAT or GCN5-related N-acetyltransferase superfamily. Although the physiological function of AAC(2’)-Ic is not certain, the crystal structure determined by the scientists allowed them to hypothesize. Through the crystal structure, scientists determined that this enzyme might acetylate mycothiol, which is a 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 scientists in the study determined the crystal structure of AAC (2’)-Ic from Mycobacterium tuberculosis. The specific fold of AAC (2’)-Ic is placed in the GNAT or GCN5-related N-acetyltransferase superfamily. Although the physiological function of AAC(2’)-Ic is not certain, the crystal structure determined by the scientists allowed them to hypothesize. Through the crystal structure, scientists determined that this enzyme might acetylate mycothiol, which is a 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.<references name="1"/> | ||
