6u7a
Rv3722c in complex with kynurenine
Structural highlights
FunctionASPAT_MYCTU Main aspartate aminotransferase that couples nitrogen assimilation to aspartate synthesis. Has a weak, but significant, side activity toward kynurenine (Kyn). Oxaloacetate and 2-oxoglutarate, but not pyruvate, serve as amino acceptors, while Asp, Glu and Kyn serve as the best amino donors. Essential for axenic growth and survival of M.tuberculosis in macrophages and in mice.[1] Publication Abstract from PubMedGene rv3722c of Mycobacterium tuberculosis is essential for in vitro growth, and encodes a putative pyridoxal phosphate-binding protein of unknown function. Here we use metabolomic, genetic and structural approaches to show that Rv3722c is the primary aspartate aminotransferase of M. tuberculosis, and mediates an essential but underrecognized role in metabolism: nitrogen distribution. Rv3722c deficiency leads to virulence attenuation in macrophages and mice. Our results identify aspartate biosynthesis and nitrogen distribution as potential species-selective drug targets in M. tuberculosis. Aspartate aminotransferase Rv3722c governs aspartate-dependent nitrogen metabolism in Mycobacterium tuberculosis.,Jansen RS, Mandyoli L, Hughes R, Wakabayashi S, Pinkham JT, Selbach B, Guinn KM, Rubin EJ, Sacchettini JC, Rhee KY Nat Commun. 2020 Apr 23;11(1):1960. doi: 10.1038/s41467-020-15876-8. PMID:32327655[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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