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

Young Ae Kim, Brent Shriver, Louis B. Hersh

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

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 (US)
Pages (from-to)883-887
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume184
Issue number2
DOIs
StatePublished - Apr 30 1992
Externally publishedYes

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Neprilysin
Histidine
Mutagenesis
Enzymes
Site-Directed Mutagenesis
Glutamine
Catalysis
Zinc
Catalyst activity
Ligands
Kinetics

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Mutational analysis reveals only one catalytic histidine in neutral endopeptidase ("enkephalinase"). / Kim, Young Ae; Shriver, Brent; Hersh, Louis B.

In: Biochemical and Biophysical Research Communications, Vol. 184, No. 2, 30.04.1992, p. 883-887.

Research output: Contribution to journalArticle

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