EC Number   |
Reaction |
Reference |
|---|
   4.6.1.18 | an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA] |
(1) overall reaction |
- |
| 4.6.1.18 | an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA] |
enzymatic reaction mechanism, analysis of different versions, e.g. mechanism of Mathias and Rabin for catalysis of the hydrolysis of cytidine 2',3'-cyclic phosphate by RNase A, overview. Model of the RNase A-substrate complex, subsites of RNase A. Bn, Rn, and Rho_n are nucleobase-, ribose-, and phosphate-binding subsites, respectively |
717258 |
| 4.6.1.18 | an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA] |
Gly38 and Glu111 are crucial for the catalytic activity |
654423 |
| 4.6.1.18 | an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA] |
His119 and His12 play an important structural role in active site of RNase A |
666170 |
| 4.6.1.18 | an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA] |
His12, His119 and Lys41 comprise the catalytic site, and several other amino acid residues serve as substrate binding subsites. The mutagenic replacement of Phe120 causes a positional change in His119 and that is a major cause in decreasing the activity of the enzyme. Phe120 is important in fixing the proper spatial position of His119 near the C-terminal region for efficient activity. Phe120 interacts not directly with His119, but with the hydrophobic core |
657293 |
| 4.6.1.18 | an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA] |
protein of 128 amino acid residues, catalyses the cleavage of RNA specifically on the 3'-side of pyrimidine bases. The catalytic triad comprises His12, Lys41 and His119. The amino acid sequence of the enzyme is longer than that of its bovine counterpart, with four extra amino acid residues at the C-terminal region |
656482 |
| 4.6.1.18 | an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA] |
protein with 124 amino acid residues and four intra-molecular disulfide bonds. In the presence of oxidized and reduced dithiothreitol at pH 8.0 and 25ºC, the enzyme folds through pathways involving a rapid pre-equilibrium resulting in an ensemble of three-disulfide intermediate species. Protein disulfide isomerase catalyzes the conversion of the intermediates to the native enzyme, by acting as both a chaperone and an oxidase on the on-pathway intermediate |
655556 |
| 4.6.1.18 | an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA] |
pyrimidine-specific endoribonuclease which cleaves 3',5'-phosphodiester bonds of single strand RNA via transphosphorylation and subsequent hydrolysis reactions |
656315 |
| 4.6.1.18 | an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA] |
RNase A catalyzes a well-characterized acid-base mechanism involving two histidines (His12 and His119) and a transition state stabilizing positive charge (Lys41). The transphosphorylation of a single-stranded RNA molecule by the enzyme yields a 2',3'-cyclic phosphomonoester intermediate, which can be expelled from the active site or hydrolyzed in a microscopic reverse reaction involving the same two histidines |
729713 |
| 4.6.1.18 | an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA] |
sequential binding of the monomeric substrate in a concentration-dependent manner makes up the active site of the enzyme |
656631 |
