Nucleoside deoxyribosyltransferase

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nucleoside deoxyribosyltransferase
Nucleoside 2-deoxyribosyltransferase homohexamer, Lactobacillus leichmannii
EC no.
CAS no.9026-86-2
IntEnzIntEnz view
ExPASyNiceZyme view
MetaCycmetabolic pathway
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

In enzymology, a nucleoside deoxyribosyltransferase (EC is an enzyme that catalyzes the chemical reaction

2-deoxy-D-ribosyl-base1 + base2 2-deoxy-D-ribosyl-base2 + base1

Thus, the two substrates of this enzyme are 2-deoxy-D-ribosyl-base1 and base2, whereas its two products are 2-deoxy-D-ribosyl-base2 and base1.

This enzyme belongs to the family of glycosyltransferases, specifically the pentosyltransferases. The systematic name of this enzyme class is nucleoside:purine(pyrimidine) deoxy-D-ribosyltransferase. Other names in common use include purine(pyrimidine) nucleoside:purine(pyrimidine) deoxyribosyl, transferase, deoxyribose transferase, nucleoside trans-N-deoxyribosylase, trans-deoxyribosylase, trans-N-deoxyribosylase, trans-N-glycosidase, nucleoside deoxyribosyltransferase I (purine nucleoside:purine, deoxyribosyltransferase: strictly specific for transfer between, purine bases), nucleoside deoxyribosyltransferase II [purine(pyrimidine), and nucleoside:purine(pyrimidine) deoxyribosyltransferase]. This enzyme participates in pyrimidine metabolism.

Structural studies[edit]

As of late 2007, 12 structures have been solved for this class of enzymes, with PDB accession codes 1F8X, 1F8Y, 1S2D, 1S2G, 1S2I, 1S2L, 1S3F, 2A0K, 2F2T, 2F62, 2F64, and 2F67.


  • KALCKAR HM, MACNUTT WS, HOFF-JORGENSEN E (1952). "Trans-N-glycosidase studied with radioactive adenine". Biochem. J. 50 (3): 397–400. doi:10.1042/bj0500397. PMC 1197666. PMID 14915963.
  • MACNUTT WS (1952). "The enzymically catalysed transfer of the deoxyribosyl group from one purine or pyrimidine to another". Biochem. J. 50 (3): 384–97. doi:10.1042/bj0500384. PMC 1197665. PMID 14915962.
  • ROUSH AH, BETZ RF (1958). "Purification and properties of trans-N-deoxyribosylase". J. Biol. Chem. 233 (2): 261–6. PMID 13563482.