The Enzyme Database

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EC 4.6.1.22     
Accepted name: Bacillus subtilis ribonuclease
Reaction: RNA = a 5′-hydroxy-ribonucleotide + n nucleoside-2′,3′-cyclophosphates
Other name(s): Proteus mirabilis RNase; ribonucleate nucleotido-2′-transferase (cyclizing); bacterial RNA lyase; Bacillus subtilis intracellular ribonuclease
Systematic name: [RNA] 5′-hydroxy-ribonucleotide-3′-[RNA fragment]-lyase (cyclicizing; [RNA fragment]-3′- nucleoside -2′,3′-cyclophosphate-forming)
Comments: This enzyme catalyses endonucleolytic cleavage to 2′,3′-cyclic nucleotides. The cyclic products may be hydrolysed to the corresponding 3′-phosphates by 2′,3′-cyclic-nucleotide 2′-phosphodiesterase (EC 3.1.4.16). The enzyme from B. subtilis is inhibited by ATP.
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB
References:
1.  Nishimura, H. and Maruo, B. Intracellular ribonuclease from Bacillus subtilis. Biochim. Biophys. Acta 40 (1960) 355–357. [DOI] [PMID: 13854124]
2.  Yamasaki, M. and Arima, K. Regulation of intracellular ribonuclease of Bacillus subtilis by ATP and ADP. Biochim. Biophys. Acta 139 (1967) 202–204. [DOI] [PMID: 4962137]
3.  Yamasaki, M. and Arima, K. Intracellular ribonuclease of Bacillus subtilis; specific inhibition by ATP and dATP. Biochem. Biophys. Res. Commun. 37 (1969) 430–436. [DOI] [PMID: 4981632]
4.  Center, M.S. and Behal, F.J. Studies on the ribonuclease activity of Proteus mirabilis. Biochim. Biophys. Acta 151 (1968) 698–699. [PMID: 4296400]
[EC 4.6.1.22 created 1978 as EC 3.1.27.2, transferred 2028 to EC 4.6.1.22]
 
 


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