Premium
Modified nucleotides as substrates and inhibitors of adenylate kinase from different sources
Author(s) -
Skoblov Juri S,
Frank-Kamenetskaya Maria D,
Chernov Dmitry N,
Krayevsky Alexander A
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)01039-3
Subject(s) - adenylate kinase , nucleotide , deoxyribonucleotides , chemistry , biochemistry , enzyme , substrate (aquarium) , escherichia coli , kinase , phosphorylation , stereochemistry , biology , gene , ecology
The substrate and inhibitory properties of modified nucleotides with respect to adenylate kinase from rabbit muscles, human placenta and Escherichia coli were studied. A number of 5′‐hydrogenphosphonates and 5′‐fluorophosphates of modified nucleotides were shown to inhibit the phosphorylation reaction catalyzed by these enzymes. A clear difference between phosphonates of 3′‐deoxyribonucleotides and the corresponding ribo‐ and 2′,3′‐dideoxyribonucleotides was found. 3′‐Azido‐2′,3′‐dideoxythymidine and its phosphorus derivatives did not inhibit the adenylate kinase reaction.