Mutational analysis reveals only one catalytic histidine in neutral endopeptidase ("enkephalinase")

Young Ae Kim, Brent Shriver, Louis B. Hersh

Research output: Contribution to journalArticlepeer-review

7 Scopus citations


Aside from serving as zinc ligands, kinetic data has implicated one or more additional histidines as catalytic residues in neutral endopeptidase ("enkephalinase") action. One of these histidines has previously been identified as histidine 704 (Bateman et al., J. Biol. Chem., 265:8365-8368, 1990). In order to determine whether a second histidine is involved in catalysis each of these residues not previously changed have been converted to glutamine by site directed mutagenesis. The resultant recombinant enzymes possess full catalytic activity indicating that histidine 704 is the only catalytic histidine in the enzyme.

Original languageEnglish
Pages (from-to)883-887
Number of pages5
JournalBiochemical and Biophysical Research Communications
Issue number2
StatePublished - Apr 30 1992

Bibliographical note

Funding Information:
This research was supported in part from and grant #I391 from the Welch Foundation,

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


Dive into the research topics of 'Mutational analysis reveals only one catalytic histidine in neutral endopeptidase ("enkephalinase")'. Together they form a unique fingerprint.

Cite this