ExplorEnz: EC 2.3.2.37

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2.3.2.37

Accepted name:

ergosteryl-3β-O-L-aspartate synthase

Reaction:

L-aspartyl-tRNA^Asp + ergosterol = tRNA^Asp + 1-(ergostan-3β-yl)-L-aspartate

Other name(s):

ErdS

Systematic name:

L-aspartyl-tRNA^Asp: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 tRNA^Asp (EC 6.1.1.12), 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

References:

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 2.3.2.37 created 2023]