[Ribonuclease Fl1 from Fusarium lateriticum. Isolation, substrate specificity and amino acid sequence].
Extracellular RNase Fl1 has been purified from the culture filtrate of Fusarium lateritium. The enzyme has been obtained in the electrophoretically homogeneous state with the yield about 90% and 300 fdd degree of purification. RNase Fl1 is a guanyl specific enzyme (EC 3.1.27.3) with the specific activity on RNA 1420 units/mg of protein. The total primary structure of the RNase has been determined by the automated Edman degradation of two non-fractionated peptide hydrolysates produced by trypsin and Staphylococcus aureus protease and of the hydroxylamine cleavage products of the protein. It was shown that hydroxylamine converts the RNase Fl1 N-terminal residue, pyroglutamic acid, into the hydroxyamic acid derivative sensitive to Edman degradation. RNase Fl1 consists of 105 amino acid residues (Mr 10,852) and is a structural homologue of the Fus. moniliforme RNase F1, differing from the latter by 15 amino acid substitutions outside the enzyme active site.
D000595:Amino Acid Sequence; D004722:Endoribonucleases / Q000302:isolation & purification*; D005670:Fusarium / Q000201:enzymology*; D006868:Hydrolysis; D007700:Kinetics; D008969:Molecular Sequence Data; D006163:Ribonuclease T1 / Q000302:isolation & purification* / Q000378:metabolism; D013379:Substrate Specificity
D004722:Endoribonucleases; D006163:Ribonuclease T1
Ribonukleaza Fl1 Fusarium lateriticum. Vydelenie, substratnaia spetsifichnost' i aminokislotnaia posledovatel'nost'.