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The c-Myc target gene Rcl (C6orf108) encodes a novel enzyme, deoxynucleoside 5'-monophosphate N-glycosidase.

Abstract : RCL is a c-Myc target with tumorigenic potential. Genome annotation predicted that RCL belonged to the N-deoxyribosyltransferase family. However, its putative relationship to this class of enzymes did not lead to its precise biochemical function. The purified native or N-terminal His-tagged recombinant rat RCL protein expressed in Escherichia coli exhibits the same enzyme activity, deoxynucleoside 5'-monophosphate N-glycosidase, never before described. dGMP appears to be the best substrate. RCL opens a new route in the nucleotide catabolic pathways by cleaving the N-glycosidic bond of deoxynucleoside 5'-monophosphates to yield two reaction products, deoxyribose 5-phosphate and purine or pyrimidine base. Biochemical studies show marked differences in the terms of the structure and catalytic mechanism between RCL and of its closest enzyme family neighbor, N-deoxyribosyltransferase. The reaction products of this novel enzyme activity have been implicated in purine or pyrimidine salvage, glycolysis, and angiogenesis, and hence are all highly relevant for tumorigenesis.
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Contributor : Alexandre Kaminski Connect in order to contact the contributor
Submitted on : Tuesday, August 7, 2007 - 12:17:13 PM
Last modification on : Thursday, May 5, 2022 - 3:18:01 PM

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Yoan Konto Ghiorghi, Karen I Zeller, Chi V Dang, Pierre-Alexandre Kaminski. The c-Myc target gene Rcl (C6orf108) encodes a novel enzyme, deoxynucleoside 5'-monophosphate N-glycosidase.. Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2007, 282 (11), pp.8150-6. ⟨10.1074/jbc.M610648200⟩. ⟨pasteur-00166562⟩



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