Crystallization (Comment) | Organism |
---|---|
crystal structure analysis, PDB ID 1RRA | Rattus norvegicus |
crystal structure analysis, PDB ID 2VQ9 | Danio rerio |
crystal structure analysis, PDB ID 3DJX | Bos taurus |
crystal structure analysis, PDB ID 3PHN | Lithobates pipiens |
crystal structure analysis, PDB IDs 1GQV, 1QMT, 1RNF, and 1ANG | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
additional information | construction of a chimeric hybrid RNase AECP variant, in which the short and rigid six-residue loop 1 from human isozyme RNase 3 replaces the 12-residue flexible loop 1 in RNase A, the mutation perturbs the flexibility of the hinge/loop 1 environment and causes a 10fold decrease in the product release rate constant koff and a 4fold decrease in ligand affinity relative to the parent enzyme | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Gallus gallus | the enzyme degrades single-stranded and/or double-stranded RNA | ? | - |
? | |
additional information | Homo sapiens | the enzyme degrades single-stranded and/or double-stranded RNA | ? | - |
? | |
additional information | Danio rerio | the enzyme degrades single-stranded and/or double-stranded RNA | ? | - |
? | |
additional information | Bos taurus | the enzyme degrades single-stranded and/or double-stranded RNA | ? | - |
? | |
additional information | Lithobates pipiens | the enzyme degrades single-stranded and/or double-stranded RNA | ? | - |
? | |
additional information | Rattus norvegicus | the enzyme degrades single-stranded and/or double-stranded RNA | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bos taurus | P00669 | isozymes RNase A and BS-RNase | - |
Danio rerio | A5HAK0 | - |
- |
Gallus gallus | - |
- |
- |
Homo sapiens | - |
- |
- |
Homo sapiens | - |
isozymes RNases 1, 2, 3, 4, and 5 | - |
Lithobates pipiens | P22069 | i.e. Pantherana pipiens | - |
Rattus norvegicus | P00684 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
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 | Gallus gallus | |
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 | Homo sapiens | |
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 | Danio rerio | |
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 | Bos taurus | |
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 | Lithobates pipiens | |
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 | Rattus norvegicus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | the enzyme degrades single-stranded and/or double-stranded RNA | Gallus gallus | ? | - |
? | |
additional information | the enzyme degrades single-stranded and/or double-stranded RNA | Homo sapiens | ? | - |
? | |
additional information | the enzyme degrades single-stranded and/or double-stranded RNA | Danio rerio | ? | - |
? | |
additional information | the enzyme degrades single-stranded and/or double-stranded RNA | Bos taurus | ? | - |
? | |
additional information | the enzyme degrades single-stranded and/or double-stranded RNA | Lithobates pipiens | ? | - |
? | |
additional information | the enzyme degrades single-stranded and/or double-stranded RNA | Rattus norvegicus | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
BS-RNase | - |
Bos taurus |
Ecp | - |
Homo sapiens |
eosinophil cationic protein | - |
Homo sapiens |
onconase | - |
Lithobates pipiens |
ranpirnase | - |
Lithobates pipiens |
RNase 1 | - |
Homo sapiens |
RNase 1 | - |
Rattus norvegicus |
RNase 2 | - |
Homo sapiens |
RNase 3 | - |
Homo sapiens |
RNase 3 | - |
Danio rerio |
RNase 4 | - |
Homo sapiens |
RNase 5 | - |
Homo sapiens |
RNase A | - |
Gallus gallus |
RNase A | - |
Homo sapiens |
RNase A | - |
Danio rerio |
RNase A | - |
Bos taurus |
RNase A | - |
Lithobates pipiens |
RNase A | - |
Rattus norvegicus |
RNase A2 | - |
Gallus gallus |
RNase ZF-3e | - |
Danio rerio |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme belongs to the vertebrate pancreatic-like RNase A superfamily, sequence comparisons and phylogenetic analysis, overview | Gallus gallus |
evolution | the enzyme belongs to the vertebrate pancreatic-like RNase A superfamily, sequence comparisons and phylogenetic analysis, overview | Homo sapiens |
evolution | the enzyme belongs to the vertebrate pancreatic-like RNase A superfamily, sequence comparisons and phylogenetic analysis, overview | Danio rerio |
evolution | the enzyme belongs to the vertebrate pancreatic-like RNase A superfamily, sequence comparisons and phylogenetic analysis, overview | Bos taurus |
evolution | the enzyme belongs to the vertebrate pancreatic-like RNase A superfamily, sequence comparisons and phylogenetic analysis, overview | Lithobates pipiens |
evolution | the enzyme belongs to the vertebrate pancreatic-like RNase A superfamily, sequence comparisons and phylogenetic analysis, overview | Rattus norvegicus |
additional information | RNA subsites and reaction mechanism catalyzed by RNase A, molecular interactions between the RNA substrate and residues of the catalytic groove. The following residues are known to interact with each subsite: Lys66 (P0), Thr45 and Asp83 (B1), Gln11, His12, Lys41, His119, and Asp121 (P1), Asn71 and Glu111 (B2), and Lys7 and Arg10 (P2). Structure-function relationship, overview | Homo sapiens |
additional information | RNA subsites and reaction mechanism catalyzed by RNase A, molecular interactions between the RNA substrate and residues of the catalytic groove. The following residues are known to interact with each subsite: Lys66 (P0), Thr45 and Asp83 (B1), Gln11, His12, Lys41, His119, and Asp121 (P1), Asn71 and Glu111 (B2), and Lys7 and Arg10 (P2). Structure-function relationship, overview. Potential role for catalytic base His119 in ligand discrimination and/or stabilization in addition to its critical role in catalysis, molecular dynamic simulations show that His119 adopts both rotameric positions in solution, most likely experiencing conformational exchange over the course of a catalytic reaction. Functional importance of long-range conformational rearrangements in RNase A | Gallus gallus |
additional information | RNA subsites and reaction mechanism catalyzed by RNase A, molecular interactions between the RNA substrate and residues of the catalytic groove. The following residues are known to interact with each subsite: Lys66 (P0), Thr45 and Asp83 (B1), Gln11, His12, Lys41, His119, and Asp121 (P1), Asn71 and Glu111 (B2), and Lys7 and Arg10 (P2). Structure-function relationship, overview. Potential role for catalytic base His119 in ligand discrimination and/or stabilization in addition to its critical role in catalysis, molecular dynamic simulations show that His119 adopts both rotameric positions in solution, most likely experiencing conformational exchange over the course of a catalytic reaction. Functional importance of long-range conformational rearrangements in RNase A | Homo sapiens |
additional information | RNA subsites and reaction mechanism catalyzed by RNase A, molecular interactions between the RNA substrate and residues of the catalytic groove. The following residues are known to interact with each subsite: Lys66 (P0), Thr45 and Asp83 (B1), Gln11, His12, Lys41, His119, and Asp121 (P1), Asn71 and Glu111 (B2), and Lys7 and Arg10 (P2). Structure-function relationship, overview. Potential role for catalytic base His119 in ligand discrimination and/or stabilization in addition to its critical role in catalysis, molecular dynamic simulations show that His119 adopts both rotameric positions in solution, most likely experiencing conformational exchange over the course of a catalytic reaction. Functional importance of long-range conformational rearrangements in RNase A | Danio rerio |
additional information | RNA subsites and reaction mechanism catalyzed by RNase A, molecular interactions between the RNA substrate and residues of the catalytic groove. The following residues are known to interact with each subsite: Lys66 (P0), Thr45 and Asp83 (B1), Gln11, His12, Lys41, His119, and Asp121 (P1), Asn71 and Glu111 (B2), and Lys7 and Arg10 (P2). Structure-function relationship, overview. Potential role for catalytic base His119 in ligand discrimination and/or stabilization in addition to its critical role in catalysis, molecular dynamic simulations show that His119 adopts both rotameric positions in solution, most likely experiencing conformational exchange over the course of a catalytic reaction. Functional importance of long-range conformational rearrangements in RNase A | Bos taurus |
additional information | RNA subsites and reaction mechanism catalyzed by RNase A, molecular interactions between the RNA substrate and residues of the catalytic groove. The following residues are known to interact with each subsite: Lys66 (P0), Thr45 and Asp83 (B1), Gln11, His12, Lys41, His119, and Asp121 (P1), Asn71 and Glu111 (B2), and Lys7 and Arg10 (P2). Structure-function relationship, overview. Potential role for catalytic base His119 in ligand discrimination and/or stabilization in addition to its critical role in catalysis, molecular dynamic simulations show that His119 adopts both rotameric positions in solution, most likely experiencing conformational exchange over the course of a catalytic reaction. Functional importance of long-range conformational rearrangements in RNase A | Lithobates pipiens |
additional information | RNA subsites and reaction mechanism catalyzed by RNase A, molecular interactions between the RNA substrate and residues of the catalytic groove. The following residues are known to interact with each subsite: Lys66 (P0), Thr45 and Asp83 (B1), Gln11, His12, Lys41, His119, and Asp121 (P1), Asn71 and Glu111 (B2), and Lys7 and Arg10 (P2). Structure-function relationship, overview. Potential role for catalytic base His119 in ligand discrimination and/or stabilization in addition to its critical role in catalysis, molecular dynamic simulations show that His119 adopts both rotameric positions in solution, most likely experiencing conformational exchange over the course of a catalytic reaction. Functional importance of long-range conformational rearrangements in RNase A | Rattus norvegicus |
physiological function | the human isozymes have evolved additional biological activities, often linked to innate host defense, neurotoxicity, angiogenesis, and immunosuppressive and/or antibacterial/antiviral activities | Homo sapiens |