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Literature summary for 4.6.1.18 extracted from

  • Doucet, N.; Jayasundera, T.; Simonovic, M.; Loria, J.
    The crystal structure of ribonuclease a in complex with thymidine-3'-monophosphate provides further insight into ligand binding (2010), Proteins, 78, 2459-2468.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
ribonuclease A in complex with thymidine 3'-monophosphate, hanging drop vapor diffusion method, 0.002 ml of 80 mg/ml protein in 20% ethanol and 20% acetic acid at pH 5.5, is mixed with 0.004 ml of 3'-TMP dissolved in a mother liquor solution of 20% ammonium sulfate and 2 M sodium chloride at pH 5.5, room temperature, 1 week, X-ray diffraction structure determination and analysis at 1.55 A resolution, molecular replacement, modelling Bos taurus

Inhibitors

Inhibitors Comment Organism Structure
3'-CMP natural product inhibitor, NMR binding analysis, overview Bos taurus
3'-TMP a competitive inhibitor analogue of the 3'-CMP and 3'-UMP natural product inhibitors, the enzyme shows very high affinty and strong binding with 3'-TMP. Binding of 3'-TMP is very similar to other natural and nonnatural pyrimidine ligands, so single nucleotide affinity is independent of the presence or absence of a 2'-hydroxyl on the ribose moiety of pyrimidines Bos taurus
3'-UMP natural product inhibitor, NMR binding analysis, overview Bos taurus
additional information enzyme-inhibitor binding and interaction analysis, kinetics, overview Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus P61823
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Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
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Bos taurus
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pancreas
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Bos taurus
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Synonyms

Synonyms Comment Organism
pancreatic ribonuclease A
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Bos taurus
RNase A
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Bos taurus

General Information

General Information Comment Organism
additional information very subtle structural, chemical, and potentially motional variations contribute to ligand discrimination in the enzyme Bos taurus