The Enzyme Database

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EC 3.4.24.25     
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 3.4.24.4
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 69598-88-5
References:
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. [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. [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. [PMID: 1551587]
[EC 3.4.24.25 created 1972 as EC 3.4.24.4, part transferred 1992 to EC 3.4.24.25, modified 1997]
 
 


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