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

Yoan Konto Ghiorghi, Karen I. Zeller, Chi V. Dang, P. Alexandre Kaminski

Research output: Contribution to journalArticle

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.

Original languageEnglish (US)
Pages (from-to)8150-8156
Number of pages7
JournalJournal of Biological Chemistry
Volume282
Issue number11
DOIs
StatePublished - Mar 16 2007

Fingerprint

myc Genes
Glycoside Hydrolases
Enzyme activity
Reaction products
Genes
Deoxyribose
Salvaging
Enzymes
Escherichia coli
Nucleotides
Phosphates
Glycolysis
Substrates
Carcinogenesis
Genome
purine
pyrimidine
rat RCL protein
2'-deoxyguanosine 5'-phosphate

ASJC Scopus subject areas

  • Biochemistry

Cite this

The c-Myc target gene Rcl (C6orf108) encodes a novel enzyme, deoxynucleoside 5′-monophosphate N-glycosidase. / Ghiorghi, Yoan Konto; Zeller, Karen I.; Dang, Chi V.; Kaminski, P. Alexandre.

In: Journal of Biological Chemistry, Vol. 282, No. 11, 16.03.2007, p. 8150-8156.

Research output: Contribution to journalArticle

Ghiorghi, Yoan Konto ; Zeller, Karen I. ; Dang, Chi V. ; Kaminski, P. Alexandre. / The c-Myc target gene Rcl (C6orf108) encodes a novel enzyme, deoxynucleoside 5′-monophosphate N-glycosidase. In: Journal of Biological Chemistry. 2007 ; Vol. 282, No. 11. pp. 8150-8156.
@article{4105e71f0e3343dc83bf0c4d42742c1f,
title = "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.",
author = "Ghiorghi, {Yoan Konto} and Zeller, {Karen I.} and Dang, {Chi V.} and Kaminski, {P. Alexandre}",
year = "2007",
month = "3",
day = "16",
doi = "10.1074/jbc.M610648200",
language = "English (US)",
volume = "282",
pages = "8150--8156",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "11",

}

TY - JOUR

T1 - The c-Myc target gene Rcl (C6orf108) encodes a novel enzyme, deoxynucleoside 5′-monophosphate N-glycosidase

AU - Ghiorghi, Yoan Konto

AU - Zeller, Karen I.

AU - Dang, Chi V.

AU - Kaminski, P. Alexandre

PY - 2007/3/16

Y1 - 2007/3/16

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=34247230158&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=34247230158&partnerID=8YFLogxK

U2 - 10.1074/jbc.M610648200

DO - 10.1074/jbc.M610648200

M3 - Article

VL - 282

SP - 8150

EP - 8156

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 11

ER -