The Enzyme Database

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Accepted name: ergosteryl-3β-O-L-aspartate synthase
Reaction: L-aspartyl-tRNAAsp + ergosterol = tRNAAsp + 1-(ergostan-3β-yl)-L-aspartate
Other name(s): ErdS
Systematic name: L-aspartyl-tRNAAsp:ergosterol-3β-O-L-aspartyltransferase
Comments: The enzyme, detected in fungal species that belong to the Ascomycota and Basidiomycota phyla and characterized from Aspergillus fumigatus, is bifunctional. The AspRS domain catalyses the transfer of L-aspartate to tRNAAsp (EC, while the second domain carries out the transfer of L-aspartate to the 3β-hydroxyl of ergosterol.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Yakobov, N., Fischer, F., Mahmoudi, N., Saga, Y., Grube, C.D., Roy, H., Senger, B., Grob, G., Tatematsu, S., Yokokawa, D., Mouyna, I., Latge, J.P., Nakajima, H., Kushiro, T. and Becker, H.D. RNA-dependent sterol aspartylation in fungi. Proc. Natl. Acad. Sci. USA 117 (2020) 14948–14957. [DOI] [PMID: 32541034]
[EC created 2023]

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