Molecular cloning of cDNA for Sarcophaga prolyl endopeptidase and characterization of the recombinant enzyme produced by an E. coli expression system

Sumio Ohtsuki; Ko Ichi Homma; Shoichiro Kurata; Shunji Natori

doi:10.1016/S0965-1748(97)00004-0

Molecular cloning of cDNA for Sarcophaga prolyl endopeptidase and characterization of the recombinant enzyme produced by an E. coli expression system

Sumio Ohtsuki, Ko Ichi Homma, Shoichiro Kurata, Shunji Natori

Research output: Contribution to journal › Article › peer-review

13 Citations (Scopus)

Abstract

A cDNA for prolyl endopeptidase (PEP) of Sarcophaga peregrina (flesh fly) was cloned and its sequence determined. The overall amino acid sequence identity between Sarcophaga and mammalian PEPs was 53%, indicating that these enzymes are structurally very similar. Northern blot hybridization revealed that the Sarcophaga PEP gene was activated significantly at the eversion stage of imaginal disc differentiation. We obtained recombinant PEP by expressing the cDNA in Escherichia coli. The recombinant and authentic enzymes showed almost identical characteristics, in terms of substrate specificities and sensitivities to inhibitors.

Original language	English
Pages (from-to)	337-343
Number of pages	7
Journal	Insect Biochemistry and Molecular Biology
Volume	27
Issue number	4
DOIs	https://doi.org/10.1016/S0965-1748(97)00004-0
Publication status	Published - 1997 Jan 1
Externally published	Yes

Keywords

Imaginal disc differentiation
Prolyl endopeptidase
Recombinant enzyme
Sarcophaga peregrina

ASJC Scopus subject areas

Insect Science
Biochemistry

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10.1016/S0965-1748(97)00004-0

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Molecular cloning of cDNA for Sarcophaga prolyl endopeptidase and characterization of the recombinant enzyme produced by an E. coli expression system. / Ohtsuki, Sumio; Homma, Ko Ichi; Kurata, Shoichiro; Natori, Shunji.

In: Insect Biochemistry and Molecular Biology, Vol. 27, No. 4, 01.01.1997, p. 337-343.

Research output: Contribution to journal › Article › peer-review

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abstract = "A cDNA for prolyl endopeptidase (PEP) of Sarcophaga peregrina (flesh fly) was cloned and its sequence determined. The overall amino acid sequence identity between Sarcophaga and mammalian PEPs was 53%, indicating that these enzymes are structurally very similar. Northern blot hybridization revealed that the Sarcophaga PEP gene was activated significantly at the eversion stage of imaginal disc differentiation. We obtained recombinant PEP by expressing the cDNA in Escherichia coli. The recombinant and authentic enzymes showed almost identical characteristics, in terms of substrate specificities and sensitivities to inhibitors.",

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AU - Ohtsuki, Sumio

AU - Homma, Ko Ichi

AU - Kurata, Shoichiro

AU - Natori, Shunji

PY - 1997/1/1

Y1 - 1997/1/1

N2 - A cDNA for prolyl endopeptidase (PEP) of Sarcophaga peregrina (flesh fly) was cloned and its sequence determined. The overall amino acid sequence identity between Sarcophaga and mammalian PEPs was 53%, indicating that these enzymes are structurally very similar. Northern blot hybridization revealed that the Sarcophaga PEP gene was activated significantly at the eversion stage of imaginal disc differentiation. We obtained recombinant PEP by expressing the cDNA in Escherichia coli. The recombinant and authentic enzymes showed almost identical characteristics, in terms of substrate specificities and sensitivities to inhibitors.

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KW - Imaginal disc differentiation

KW - Prolyl endopeptidase

KW - Recombinant enzyme

KW - Sarcophaga peregrina

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Molecular cloning of cDNA for Sarcophaga prolyl endopeptidase and characterization of the recombinant enzyme produced by an E. coli expression system

Abstract

Keywords

ASJC Scopus subject areas

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