The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

Accepted name: vibriolysin
Reaction: Preferential cleavage of bonds with bulky hydrophobic groups in P2 and P1′. Phe at P1′ is the most favoured residue, which distinguished this enzyme from thermolysin
Other name(s): Aeromonas proteolytica neutral proteinase; aeromonolysin
Comments: Thermostable enzyme from Vibrio proteolyticus (formerly Aeromonas proteolytica). Specificity related to, but distinct from, those of thermolysin and bacillolysin [1]. A zinc metallopeptidase in family M4 (thermolysin family). Formerly included in EC
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 69598-88-5
1.  Holmquist, B. and Vallee, B.L. Esterase activity of zinc neutral proteases. Biochemistry 15 (1976) 101–107. [PMID: 2276]
2.  Wilkes, S.H. and Prescott, J.M. Aeromonas neutral protease. Methods Enzymol. 45 (1976) 404–415. [DOI] [PMID: 1012006]
3.  Bayliss, M.E., Wilkes, S.H. and Prescott, J.M. Aeromonas neutral protease: specificity toward extended substrates. Arch. Biochem. Biophys. 204 (1980) 214–219. [DOI] [PMID: 7000005]
4.  Wilkes, S.H., Bayliss, M.E. and Prescott, J.M. Critical ionizing groups in Aeromonas neutral protease. J. Biol. Chem. 263 (1988) 1821–1825. [PMID: 3123480]
5.  David, V.A., Deutch, A.H., Sloma, A., Pawlyk, D., Ally, A. and Durham, D.R. Cloning, sequencing and expression of the gene encoding the extracellular neutral protease, vibriolysin, of Vibrio proteolyticus. Gene 112 (1992) 107–112. [DOI] [PMID: 1551587]
[EC created 1972 as EC, part transferred 1992 to EC, modified 1997]

Data © 2001–2024 IUBMB
Web site © 2005–2024 Andrew McDonald