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

ABSTRACT: 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.

SUBMITTER: Navratna V

PROVIDER: S-EPMC3818036 | biostudies-literature | 2013 Nov

REPOSITORIES: biostudies-literature

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

Navratna Vikas V Gopal Balasubramanian B

Acta crystallographica. Section F, Structural biology and crystallization communications 20131017 Pt 11

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 ...[more]

PMID: 24192352

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