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. 1977 May 1;163(2):385–387. doi: 10.1042/bj1630385

The role of the imidazolyl nitrogen atoms of histidine-12 in ribonuclease S.

O D van Batenburg, I Voskuyl-Holtkamp, C Schattenkerk, K Hoes, K E Kerling, E Havinga
PMCID: PMC1164708  PMID: 869932

Abstract

S-peptide (residues 1--14) analogues in which the active histidine-12 residue is replaced by Npi-methyl-L-histidine, Ntau-methyl-L-histidine and beta-(pyrid-3-yl)-L-alanine were synthesized and tested for their capacity to bind to S-protein and to activate it. The results show that both imidazolyl nitrogen atoms are required for optimal catalytic functioning, Ntau being essential to the catalytic reaction itself, Npi playing a role in keeping the imidazole ring in the correct position.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Dunn B. M., DiBello C., Kirk K. L., Cohen L. A., Chaiken I. M. Synthesis, purification, and properties of a semisynthetic ribonuclease S incorporating 4-fluoro-L-histidine at position 12. J Biol Chem. 1974 Oct 10;249(19):6295–6301. [PubMed] [Google Scholar]
  2. Findlay D., Herries D. G., Mathias A. P., Rabin B. R., Ross C. A. The active site and mechanism of action of bovine pancreatic ribonuclease. 7. The catalytic mechanism. Biochem J. 1962 Oct;85(1):152–153. doi: 10.1042/bj0850152. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Hofmann K., Visser J. P., Finn F. M. Studies on polypepides. XLIV. Potent synthetic S-peptide antagonists. J Am Chem Soc. 1970 May 6;92(9):2900–2909. doi: 10.1021/ja00712a049. [DOI] [PubMed] [Google Scholar]
  4. Merrifield R. B. Solid-phase peptide synthesis. Adv Enzymol Relat Areas Mol Biol. 1969;32:221–296. doi: 10.1002/9780470122778.ch6. [DOI] [PubMed] [Google Scholar]
  5. Patel D. J., Canuel L. L., Woodward C., Bovey F. A. Assignment of the histidine 12-threonine 45 hydrogen-bonded proton in the NMR spectrum of ribonuclease A in H2O. Biopolymers. 1975 May;14(5):959–974. doi: 10.1002/bip.1975.360140506. [DOI] [PubMed] [Google Scholar]
  6. Roberts G. C., Dennis E. A., Meadows D. H., Cohen J. S., Jardetzky O. The mechanism of action of ribonuclease. Proc Natl Acad Sci U S A. 1969 Apr;62(4):1151–1158. doi: 10.1073/pnas.62.4.1151. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Usher D. A., Erenrich E. S., Eckstein F. Geometry of the first step in the action of ribonuclease-A (in-line geometry-uridine2',3'-cyclic thiophosphate- 31 P NMR). Proc Natl Acad Sci U S A. 1972 Jan;69(1):115–118. doi: 10.1073/pnas.69.1.115. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Van Batenburg O. D., Kerling K. E., Havinga E. Synthesis and enzymatic activity of an RNase S' analogue in which the 4-imidazolylglycyl residue takes the position and the role of histidine-12. FEBS Lett. 1976 Oct 1;68(2):228–230. doi: 10.1016/0014-5793(76)80442-5. [DOI] [PubMed] [Google Scholar]
  9. Voskuyl-Holtkamp I., Schattenkerk C., Havinga E. Studies on polypeptides. Int J Pept Protein Res. 1976;8(5):455–458. [PubMed] [Google Scholar]
  10. Woodfin B. M., Massey V. Spectrophotometric determination of the dissociation constant of ribonuclease S'. J Biol Chem. 1968 Mar 10;243(5):889–892. [PubMed] [Google Scholar]
  11. van Batenburg O. D., Kerling K. E. An improved synthesis of tert-butyloxycarbonyl-L-histidine. Int J Pept Protein Res. 1976;8(1):1–2. doi: 10.1111/j.1399-3011.1976.tb02473.x. [DOI] [PubMed] [Google Scholar]

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