Oxyanion hole

from Wikipedia, the free encyclopedia
Oxyanion hole in the active center of a serine protease (black) with stabilization of the substrate (red) by the protein backbone (blue)

The oxyanion hole is a form of the active center of enzymes in which a negatively charged oxygen (an oxyanion) is bound and stabilized. The oxyanion hole occurs in some dehydrogenases (in the mannitol-2-dehydrogenase from Pseudomonas fluorescens ) and some esterases , including serine proteases , cysteine ​​proteases , lipases and acyltransferases . The oxyanion hole forms a suitable gap in the active center and stabilizes the negatively charged ( anionic ) form of oxygen (oxy), which here represents the transition state of the substrate , in the course of enzymatic catalysis . Correspondingly, the activation energy of the reaction is lowered in catalysis .

In the course of protein design , the oxyanion hole was modified to use a protease for protein ligation .

literature

  • EV Beletskiy, J. Schmidt, XB Wang, SR Kass: Three hydrogen bond donor catalysts: oxyanion hole mimics and transition state analogues. In: JACS . Volume 134, number 45, November 2012, pp. 18534-18537, doi : 10.1021 / ja3085862 , PMID 23113730 .

Individual evidence

  1. ↑ M. Klimacek, B. Nidetzky: The oxyanion hole of Pseudomonas fluorescens mannitol 2-dehydrogenase: a novel structural motif for electrostatic stabilization in alcohol dehydrogenase active sites. In: Biochemical Journal . Volume 425, Number 2, January 2010, pp. 455-463, doi : 10.1042 / BJ20091441 , PMID 19857201 .
  2. ^ A b R. Ménard, AC Storer: Oxyanion hole interactions in serine and cysteine ​​proteases. In: Biological Chemistry Hoppe-Seyler. Volume 373, Number 7, July 1992, pp. 393-400, PMID 1387535 .
  3. ↑ S. Canaan, A. Roussel, R. Verger, C. Cambillau: Gastric lipase: crystal structure and activity. In: Biochimica et Biophysica Acta . Volume 1441, Numbers 2-3, November 1999, pp. 197-204, PMID 10570247 .
  4. ↑ A. Bassegoda, FI Pastor, P. Diaz: Rhodococcus sp. strain CR-53 LipR, the first member of a new bacterial lipase family (family X) displaying an unusual Y-type oxyanion hole, similar to the Candida antarctica lipase clan. In: Applied and Environmental Microbiology . Volume 78, number 6, March 2012, pp. 1724-1732, doi : 10.1128 / AEM.06332-11 , PMID 22226953 , PMC 3298128 (free full text).
  5. ↑ C. Milkowski, D. Strack: Serine carboxypeptidase-like acyltransferases. In: Phytochemistry . Volume 65, Number 5, March 2004, pp. 517-524, doi : 10.1016 / j.phytochem.2003.12.018 , PMID 15003414 .
  6. ^ L. Franke, S. Liebscher, F. Bordusa: Engineering the oxyanion hole of trypsin for promoting the reverse of proteolysis. In: Journal of Peptide Science Volume 20, Number 2, February 2014, pp. 128-136, doi : 10.1002 / psc.2597 , PMID 24357225 .