HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Hoglund, L. Articles by Reichard, P. Search for Related Content PubMed PubMed Citation Articles by Hoglund, L. Articles by Reichard, P. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 265, Issue 12, 6589-6595, 04, 1990

Cytoplasmic 5'(3')-nucleotidase from human placenta

L Hoglund and P Reichard
Department of Biochemistry I, Medical Nobel Institute, Karolinska Institutet, Stockholm, Sweden.

The 5'(3')-nucleotidase earlier partially purified from rat liver by Fritzson and Smith [1971) Biochim. Biophys. Acta 235, 128-141) was purified 15,000-fold to apparent homogeneity from human placenta. The soluble enzyme is a homodimer with a native molecular mass of 44-45 kDa. It has a pH optimum between 6.0 and 6.5 and is absolutely dependent on Mg2+ ions. The enzyme dephosphorylates certain 2'-, 3'-, and 5'-nucleotides. Km values for 2'- and 3'-nucleotides are around 0.3 mM with no preference for either ribo- or deoxyribonucleotides. 5'- Deoxyribonucleotides are 10-fold better substrates than the corresponding ribonucleotides, with dIMP greater than dUMP greater than dGMP greater than dTMP. dAMP is a poor substrate, dCMP is essentially insert. In all cases the Km values are in the millimolar range. Of the different forms of nucleotidases characterized in animal cells, the 5'(3')-nucleotidase is unique in its preference for 5'- deoxyribonucleotides. In intact cells, a portion of de novo synthesized deoxyribonucleotides is degraded as part of a homeostatic mechanism regulating the size of deoxyribonucleotide pools. This requires the participation of one or several 5'-nucleotidases. The 5'(3')- nucleotidase may be one such enzyme.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				K. Wallden, P. Stenmark, T. Nyman, S. Flodin, S. Graslund, P. Loppnau, V. Bianchi, and P. Nordlund Crystal Structure of Human Cytosolic 5'-Nucleotidase II: INSIGHTS INTO ALLOSTERIC REGULATION AND SUBSTRATE RECOGNITION J. Biol. Chem., June 15, 2007; 282(24): 17828 - 17836. [Abstract] [Full Text] [PDF]

				V. Bianchi and J. Spychala Mammalian 5'-Nucleotidases J. Biol. Chem., November 21, 2003; 278(47): 46195 - 46198. [Full Text] [PDF]

				L. Gallinaro, K. Crovatto, C. Rampazzo, G. Pontarin, P. Ferraro, E. Milanesi, P. Reichard, and V. Bianchi Human Mitochondrial 5'-Deoxyribonucleotidase. OVERPRODUCTION IN CULTURED CELLS AND FUNCTIONAL ASPECTS J. Biol. Chem., September 13, 2002; 277(38): 35080 - 35087. [Abstract] [Full Text] [PDF]

				J. Balzarini, S. Aquaro, T. Knispel, C. Rampazzo, V. Bianchi, C.-F. Perno, E. De Clercq, and C. Meier Cyclosaligenyl-2',3'-didehydro-2',3'-dideoxythymidine Monophosphate: Efficient Intracellular Delivery of d4TMP Mol. Pharmacol., November 1, 2000; 58(5): 928 - 935. [Abstract] [Full Text]

				C. Rampazzo, M. Johansson, L. Gallinaro, P. Ferraro, U. Hellman, A. Karlsson, P. Reichard, and V. Bianchi Mammalian 5'(3')-Deoxyribonucleotidase, cDNA Cloning, and Overexpression of the Enzyme in Escherichia coli and Mammalian Cells J. Biol. Chem., February 25, 2000; 275(8): 5409 - 5415. [Abstract] [Full Text] [PDF]

				S. Allegrini, A. Scaloni, L. Ferrara, R. Pesi, P. Pinna, F. Sgarrella, M. Camici, S. Eriksson, and M. G. Tozzi Bovine Cytosolic 5'-Nucleotidase Acts through the Formation of an Aspartate 52-Phosphoenzyme Intermediate J. Biol. Chem., August 31, 2001; 276(36): 33526 - 33532. [Abstract] [Full Text] [PDF]