Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1990 Mar 15;266(3):771–775. doi: 10.1042/bj2660771

High-efficiency transpeptidation catalysed by clostripain and electrostatic effects in substrate specificity.

S Yagisawa 1, S Watanabe 1, T Takaoka 1, H Azuma 1
PMCID: PMC1131206  PMID: 2327965

Abstract

Clostripain catalyses the transpeptidation between benzoylarginin ethyl ester and amino acid amides, oligopeptides, insulin A- and B-chains and tryptic peptides of myoglobin at millimolar substrate concentrations. The reactions proceed with temporary accumulation of the products, followed by hydrolytic decomposition. The yield was not affected significantly by the type of N-terminal amino acid, but was diminished markedly by the negative charges of the amine components. The yields for natural peptides were linearly related to the charge density of the peptides.

Full text

PDF
771

Selected References

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

  1. Chaiken I. M. Semisynthetic peptides and proteins. CRC Crit Rev Biochem. 1981;11(3):255–301. doi: 10.3109/10409238109108703. [DOI] [PubMed] [Google Scholar]
  2. Dixon H. B., Perham R. N. Reversible blocking of amino groups with citraconic anhydride. Biochem J. 1968 Sep;109(2):312–314. doi: 10.1042/bj1090312. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Fields R. The measurement of amino groups in proteins and peptides. Biochem J. 1971 Sep;124(3):581–590. doi: 10.1042/bj1240581. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Homandberg G. A., Komoriya A., Chaiken I. M. Enzymatic condensation of nonassociated peptide fragments using a molecular trap. Biochemistry. 1982 Jul 6;21(14):3385–3389. doi: 10.1021/bi00257a021. [DOI] [PubMed] [Google Scholar]
  5. Juillerat M., Homandberg G. A. Clostripain-catalyzed re-formation of a peptide bond in a cytochrome C fragment complex. Int J Pept Protein Res. 1981 Oct;18(4):335–342. doi: 10.1111/j.1399-3011.1981.tb02990.x. [DOI] [PubMed] [Google Scholar]
  6. Juliano L., Paiva A. C. Conformation of angiotensin II in aqueous solution. Titration of several peptide analogs and homologs. Biochemistry. 1974 May 21;13(11):2445–2450. doi: 10.1021/bi00708a032. [DOI] [PubMed] [Google Scholar]
  7. Matthew J. B., Gurd F. R. Calculation of electrostatic interactions in proteins. Methods Enzymol. 1986;130:413–436. doi: 10.1016/0076-6879(86)30019-3. [DOI] [PubMed] [Google Scholar]
  8. NILSSON K. K., FRUTON J. S. POLYMERIZATION REACTIONS CATALYZED BY INTRACELLULAR PROTEINASES. IV. FACTORS INFLUENCING THE POLYMERIZATION OF DIPEPTIDE AMIDES BY CATHEPSIN C. Biochemistry. 1964 Sep;3:1220–1224. doi: 10.1021/bi00897a006. [DOI] [PubMed] [Google Scholar]
  9. Proudfoot A. E., Offord R. E., Rose K., Schmidt M., Wallace C. J. A case of spurious product formation during attempted resynthesis of proteins by reverse proteolysis. Some batches of 'pure' glycerol contain cross-linking agents. Biochem J. 1984 Jul 15;221(2):325–331. doi: 10.1042/bj2210325. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Sahni G., Cho Y. J., Iyer K. S., Khan S. A., Seetharam R., Acharya A. S. Semisynthetic hemoglobin A: reconstitution of functional tetramer from semisynthetic alpha-globin. Biochemistry. 1989 Jun 27;28(13):5456–5461. doi: 10.1021/bi00439a021. [DOI] [PubMed] [Google Scholar]
  11. Sanger F. The free amino groups of insulin. Biochem J. 1945;39(5):507–515. doi: 10.1042/bj0390507. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Yagisawa S. Studies on protein semisynthesis. I. Formation of esters, hydrazides, and substituted hydrazides of peptides by the reverse reaction of trypsin. J Biochem. 1981 Feb;89(2):491–501. doi: 10.1093/oxfordjournals.jbchem.a133224. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES