A structure-based site-directed mutagenesis study on the neurolysin (EC 3.4.24.16) and thimet oligopeptidase (EC 3.4.24.15) catalysis

FEBS Lett. 2003 Apr 24;541(1-3):89-92. doi: 10.1016/s0014-5793(03)00310-7.

Abstract

Neurolysin (EP24.16) and thimet oligopeptidase (EP24.15) are closely related metalloendopeptidases. Site-directed mutagenesis of Tyr(613) (EP24.16) or Tyr(612) (EP24.15) to either Phe or Ala promoted a strong reduction of k(cat)/K(M) for both enzymes. These data suggest the importance of both hydroxyl group and aromatic ring at this specific position during substrate hydrolysis by these peptidases. Furthermore, the EP24.15 A607G mutant showed a k(cat)/K(M) of 2x10(5) M(-1) s(-1) for the Abz-GFSIFRQ-EDDnp substrate, similar to that of EP24.16 (k(cat)/K(M)=3x10(5) M(-1) s(-1)) which contains Gly at the corresponding position; the wild type EP24.15 has a k(cat)/K(M) of 2.5x10(4) M(-1) s(-1) for this substrate.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alanine / genetics
  • Alanine / physiology
  • Animals
  • Binding Sites
  • Catalysis
  • Kinetics
  • Metalloendopeptidases / chemistry*
  • Metalloendopeptidases / genetics
  • Metalloendopeptidases / metabolism*
  • Models, Molecular
  • Mutagenesis, Site-Directed
  • Structure-Activity Relationship
  • Substrate Specificity
  • Tyrosine / genetics
  • Tyrosine / physiology

Substances

  • Tyrosine
  • Metalloendopeptidases
  • thimet oligopeptidase
  • neurolysin
  • Alanine