A comparative study on the catalytic properties of guanyl-specific ribonucleases.
The kinetic parameters of reactions catalyzed by four guanyl-specific RNases T1, Pb1, Th1 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.
Yakovlev
G I
GI
Engelhardt Institute of Molecular Biology, USSR Academy of Sciences, Moscow.
Moiseyev
G P
GP
Bezborodova
S I
SI
Both
V
V
Sevcik
J
J
D000595:Amino Acid Sequence; D001236:Aspergillus oryzae / Q000201:enzymology; D006152:Cyclic GMP / Q000378:metabolism; D006150:Guanine Nucleotides; D006151:Guanosine / Q000378:metabolism*; D007700:Kinetics; D008969:Molecular Sequence Data; D010407:Penicillium / Q000201:enzymology; D011131:Polyribonucleotides / Q000378:metabolism; D012260:Ribonucleases / Q000737:chemistry / Q000378:metabolism*; D012689:Sequence Homology, Nucleic Acid; D013304:Streptomyces aureofaciens / Q000201:enzymology; D013379:Substrate Specificity; D014242:Trichoderma / Q000201:enzymology
D006150:Guanine Nucleotides; D011131:Polyribonucleotides; D006151:Guanosine; D012260:Ribonucleases; D006152:Cyclic GMP