[Study of splitting dinucleoside monophosphates by Penicillium brevicompactum RNAse].
In studies of splitting of transferase substrates cytidylyl-(3' leeds to 5')-adenosine and adenylyl-(3'leds to to 5')-cytidine by Penicillium brevicompactum RNAase the pH-optimum activity of enzyme has been found to fall within the range of 4.7 +/- 0;1; temperature optimum--within 41 degrees--43 degrees C; adenine-nucleotides, their constituent components and polyphosphates display the properties of competitive inhibitors on splitting substrates and that amino-acid residues (presumably weakly-  and strongly-protonated imidasole groups) function in the active site of this enzyme (pK 5.88 +/- 0,1 AND 6.6 +/- 0.1). A comparison of some physico-chemical and kinetic parameters of Penicillium breviocompactum RNAse to those of other nonspecific RNAses of fungi is made.
D000227:Adenine Nucleotides / Q000378:metabolism; D000241:Adenosine / Q000378:metabolism; D001665:Binding Sites; D003562:Cytidine / Q000378:metabolism; D003597:Cytosine Nucleotides / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D010407:Penicillium / Q000201:enzymology*; D012260:Ribonucleases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D012265:Ribonucleotides / Q000378:metabolism*; D013329:Structure-Activity Relationship; D013696:Temperature
D000227:Adenine Nucleotides; D003597:Cytosine Nucleotides; D012265:Ribonucleotides; D003562:Cytidine; D012260:Ribonucleases; D000241:Adenosine
Issledovanie rasshchepleniia RNKazoĭ Penicillium brevicompactum dinukleozidmonofosfatov