Molecular identification of N-acetylaspartylglutamate synthase and beta-citrylglutamate synthase.

The Journal of Biological Chemistry
François CollardEmile van Schaftingen

Abstract

The purpose of the present work was to determine the identity of the enzymes that synthesize N-acetylaspartylglutamate (NAAG), the most abundant dipeptide present in vertebrate central nervous system (CNS), and β-citrylglutamate, a structural analogue of NAAG present in testis and immature brain. Previous evidence suggests that NAAG is not synthesized on ribosomes but presumably is synthesized by a ligase. As attempts to detect this ligase in brain extracts failed, we searched the mammalian genomes for putative enzymes that could catalyze this type of reaction. Mammalian genomes were found to encode two putative ligases homologous to Escherichia coli RIMK, which ligates glutamates to the C terminus of ribosomal protein S6. One of them, named RIMKLA, is almost exclusively expressed in the CNS, whereas RIMKLB, which shares 65% sequence identity with RIMKLA, is expressed in CNS and testis. Both proteins were expressed in bacteria or HEK293T cells and purified. RIMKLA catalyzed the ATP-dependent synthesis of N-acetylaspartylglutamate from N-acetylaspartate and l-glutamate. RIMKLB catalyzed this reaction as well as the synthesis of β-citrylglutamate. The nature of the reaction products was confirmed by mass spectrometry and NMR. RIM...Continue Reading

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Citations

Feb 4, 2011·Proceedings of the National Academy of Sciences of the United States of America·Zachary J ReitmanHai Yan
Sep 13, 2011·The Journal of Biological Chemistry·François CollardEmile Van Schaftingen
Jul 31, 2013·The Biochemical Journal·Julia Lodder-GadaczekMatthias Eckhardt
Apr 26, 2016·Cancer & Metabolism·Daniel WeindlKarsten Hiller
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Apr 2, 2011·The Journal of Biological Chemistry·Julia Lodder-GadaczekMatthias Eckhardt
Feb 27, 2021·Scientific Reports·Koji MaekuraMasaoki Takano
Feb 28, 2021·Journal of Neurochemistry·Ivonne BeckerMatthias Eckhardt

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