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, 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] |
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[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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