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

Young Ae Kim; Brent Shriver; Louis B. Hersh

doi:10.1016/0006-291X(92)90673-9

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

Young Ae Kim, Brent Shriver, Louis B. Hersh

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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 language	English
Pages (from-to)	883-887
Number of pages	5
Journal	Biochemical and Biophysical Research Communications
Volume	184
Issue number	2
DOIs	https://doi.org/10.1016/0006-291X(92)90673-9
State	Published - Apr 30 1992

Bibliographical note

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

Funding

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

Funders	Funder number
National Institute on Drug Abuse	R01DA002243
Welch Foundation

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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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.",

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AU - Kim, Young Ae

AU - Shriver, Brent

AU - Hersh, Louis B.

N1 - Funding Information: This research was supported in part from and grant #I391 from the Welch Foundation,

PY - 1992/4/30

Y1 - 1992/4/30

N2 - 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.

AB - 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.

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

Abstract

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