His507 of acylaminoacyl peptidase stabilizes the active site conformation, not the catalytic intermediate

András L. Kiss, Z. Szeltner, Vilmos Fülöp, L. Polgár

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

Acylaminoacyl peptidase is a member of the prolyl oligopeptidase family. Amino acid sequence alignment suggests that the stabilization of the tetrahedral intermediate should be mediated by His507 rather than by a tyrosine residue found in the other family members of this serine peptidase group. The pH dependence of kcat/Km did not reveal any effect of His507. Substitution of an alanine for His507 gave the same bell-shaped pH rate profile with the same pKa values (7.0 and 8.7). However, the value of the rate constant was 85 times lower with the modified enzyme, which indicated that His507 is an important residue that is probably involved in the formation of the 3-dimensional structure.

Original languageEnglish
Pages (from-to)17-20
Number of pages4
JournalFEBS Letters
Volume571
Issue number1-3
DOIs
Publication statusPublished - Jul 30 2004

Fingerprint

prolyl oligopeptidase
Alanine
Serine
Tyrosine
Conformations
Rate constants
Catalytic Domain
Peptide Hydrolases
Substitution reactions
Stabilization
Amino Acids
Sequence Alignment
Enzymes
Amino Acid Sequence
acylaminoacyl-peptidase

Keywords

  • Acylaminoacyl peptidase
  • Catalytic mechanism
  • EDTA, ethylenediaminetetraacetic acid
  • Oligopeptidase
  • Oxyanion binding site
  • PCR, polymerase chain reaction

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

His507 of acylaminoacyl peptidase stabilizes the active site conformation, not the catalytic intermediate. / Kiss, András L.; Szeltner, Z.; Fülöp, Vilmos; Polgár, L.

In: FEBS Letters, Vol. 571, No. 1-3, 30.07.2004, p. 17-20.

Research output: Contribution to journalArticle

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AU - Fülöp, Vilmos

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