Open AccessA comparative study on the catalytic properties of guanyl‐specific ribonucleases
Author(s) -
YAKOVLEV Gennady I.,
MOISEYEV Gennady P.,
BEZBORODOVA Svetlana I.,
BOTH Valentin,
SEVCIK Jozef
Publication year - 1992
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1992.tb16622.x
Subject(s) - guanosine , catalysis , active site , stereochemistry , amino acid residue , chemistry , combinatorial chemistry , biochemistry , amino acid , peptide sequence , gene
The kinetic parameters of reactions catalyzed by four guanyl‐specific RNases T 1 , Pb 1 , Th 1 and Sa were studied comparatively using three types of substrates; guanosine‐2′,3′‐cyclophosphates, GpN dinucleoside phosphates and synthetic polyribonucleotides. The kinetic parameters were shown to be similar in spite of considerable differences in primary structures of these RNases, including amino acid residues of the active sites. Therefore, primary structures of guanyl RNases allow for a considerable number of substitutions (both in the ‘recognising’ and catalytical parts of the active site) without changes in the catalytical parameters.