Nucleotide ester-forming alcoholytic activities of nucleotide pyrophosphatases: implications for practical biotransformation, enzyme mechanisms and biological function

Citation
Jc. Cameselle et al., Nucleotide ester-forming alcoholytic activities of nucleotide pyrophosphatases: implications for practical biotransformation, enzyme mechanisms and biological function, J MOL CAT B, 11(4-6), 2001, pp. 469-485
Citations number
43
Categorie Soggetti
Physical Chemistry/Chemical Physics
Journal title
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
ISSN journal
13811177 → ACNP
Volume
11
Issue
4-6
Year of publication
2001
Pages
469 - 485
Database
ISI
SICI code
1381-1177(20010122)11:4-6<469:NEAAON>2.0.ZU;2-F
Abstract
Nucleotide pyrophosphatases (NPP) hydrolyze phosphoanhydride and phosphodie ster derivatives of nucleoside 5'-monophosphates (NMP) yielding NMP as a pr oduct. In a water-alcohol mixture, the alcohol (R-OH) competes and substitu tes for water as the splitting agent, so a mixture of NMP and NMP-O-alkyl e ster (NMP-O-R) is formed. NPPs from snake venom, potato tuber and mammalian tissues have been studied in this regard. Snake and potato NPPs were consi dered as possible practical biocatalysts to synthesize NMP-O-Rs from variou s nucleotidic substrates and alcohols. Mammalian NPPs, mainly from human bl ood and rat Liver, were studied considering the possibility that the alcoho lytic reactions catalyzed by them could be biologically relevant. Valuable information on the active centers and catalytic mechanisms of NPPs was also obtained. (C) 2001 Elsevier Science B.V. All rights reserved.