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Crystallization and preliminary X-ray diffraction studies of Staphylococcus aureus homoserine dehydrogenase

机译:金黄色葡萄球菌高丝氨酸脱氢酶的结晶和初步X射线衍射研究

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摘要

Staphylococcus aureus is a Gram-positive nosocomial pathogen. The prevalence of multidrug-resistant S. aureus strains in both hospital and community settings makes it imperative to characterize new drug targets to combat S. aureus infections. In this context, enzymes involved in cell-wall maintenance and essential amino-acid biosynthesis are significant drug targets. Homoserine dehydrogenase (HSD) is an oxidoreductase that is involved in the reversible conversion of l-aspartate semialdehyde to l-homoserine in a dinucleotide cofactor-dependent reduction reaction. HSD is thus a crucial intermediate enzyme linked to the biosynthesis of several essential amino acids such as lysine, methionine, isoleucine and threonine.
机译:金黄色葡萄球菌是革兰氏阳性医院病原体。在医院和社区环境中,多药耐药的金黄色葡萄球菌菌株的流行使得必须对付新的药物靶标以对抗金黄色葡萄球菌感染。在这种情况下,参与细胞壁维持和必需氨基酸生物合成的酶是重要的药物靶标。同型丝氨酸脱氢酶(HSD)是一种氧化还原酶,在二核苷酸辅因子依赖性还原反应中,参与了I-天冬氨酸半醛向L-高丝氨酸的可逆转化。因此,HSD是与几种必需氨基酸如赖氨酸,蛋氨酸,异亮氨酸和苏氨酸的生物合成相关的关键中间酶。

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