Structural highlights
Publication Abstract from PubMedAspartate-semialdehyde dehydrogenase (ASADH) functions at a critical junction in the aspartate biosynthetic pathway and represents a validated target for antimicrobial drug design. This enzyme catalyzes the NADPH-dependent reductive dephosphorylation of beta-aspartyl phosphate to produce the key intermediate aspartate semialdehyde. The absence of this entire pathway in humans and other mammals will allow the selective targeting of pathogenic microorganisms for antimicrobial development. Here, the X-ray structure of a new form of ASADH from the pathogenic fungal species Aspergillus fumigatus has been determined. The overall structure of this enzyme is similar to those of its bacterial orthologs, but there are some critical differences both in biological assembly and in secondary-structural features that can potentially be exploited for the development of species-selective drugs with selective toxicity against infectious fungal organisms. Structure of a fungal form of aspartate-semialdehyde dehydrogenase from Aspergillus fumigatus.,Dahal GP, Viola RE Acta Crystallogr F Struct Biol Commun. 2017 Jan 1;73(Pt 1):36-44. doi:, 10.1107/S2053230X16020070. Epub 2017 Jan 1. PMID:28045392[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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