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Photoreactivating enzyme from Escherichia coli

Journal Article:

Abstract

Escherichia coli photoreactivating enzyme (PRE) has been purified in large amounts from an E.coli strain lysogenic for a defective lambda bacteriophage carrying the phr gene. The resulting enzyme had a pH optimum of 7.2 and an ionic strength optimum of 0.18. It consisted of an apoprotein and cofactor, both of which were necessary for catalytic activity. The apoprotein had a monomer molecular weight of 35,200 and showed stable aggregates under denaturing conditions. The amino acid analysis of the E.coli enzyme was very similar to that of the photoreactivating enzyme from orchid seedlings (Cattelya aurantiaca). Both had arginine at the amino terminus. The cofactor, like the holoenzyme, showed absorption, magnetic circular dichroism, and emission properties indicative of an adenine moiety. Although the isolated enzyme had an action spectrum which peaked at about 360 nm, neither the cofactor, apoenzyme nor holoenzyme showed any detectable absorption between 300 and 400 nm.
Authors:
Snapka, R M; Fuselier, C O [1] 
  1. California Univ., Irvine (USA)
Publication Date:
May 01, 1977
Product Type:
Journal Article
Reference Number:
AIX-08-321392; EDB-77-134391
Resource Relation:
Journal Name: Photochem. Photobiol.; (United Kingdom); Journal Volume: 25:5
Subject:
63 RADIATION, THERMAL, AND OTHER ENVIRON. POLLUTANT EFFECTS ON LIVING ORGS. AND BIOL. MAT.; ESCHERICHIA COLI; PHOTOREACTIVATION; ENZYMES; ARGININE; CATALYSIS; COENZYMES; METABOLISM; MOLECULAR STRUCTURE; MOLECULAR WEIGHT; NEAR ULTRAVIOLET RADIATION; PH VALUE; PROTEIN DENATURATION; PURIFICATION; STRUCTURAL CHEMICAL ANALYSIS; ULTRAVIOLET SPECTRA; AMINO ACIDS; BACTERIA; BIOLOGICAL RECOVERY; BIOLOGICAL REPAIR; CARBOXYLIC ACIDS; ELECTROMAGNETIC RADIATION; MICROORGANISMS; ORGANIC ACIDS; ORGANIC COMPOUNDS; RADIATIONS; RECOVERY; REPAIR; SPECTRA; ULTRAVIOLET RADIATION; 560131* - Radiation Effects on Microorganisms- Basic Studies- (-1987)
OSTI ID:
7304867
Country of Origin:
United Kingdom
Language:
English
Other Identifying Numbers:
Journal ID: CODEN: PHCBA
Submitting Site:
INIS
Size:
Pages: 415-420
Announcement Date:

Journal Article:

Citation Formats

Snapka, R M, and Fuselier, C O. Photoreactivating enzyme from Escherichia coli. United Kingdom: N. p., 1977. Web.
Snapka, R M, & Fuselier, C O. Photoreactivating enzyme from Escherichia coli. United Kingdom.
Snapka, R M, and Fuselier, C O. 1977. "Photoreactivating enzyme from Escherichia coli." United Kingdom.
@misc{etde_7304867,
title = {Photoreactivating enzyme from Escherichia coli}
author = {Snapka, R M, and Fuselier, C O}
abstractNote = {Escherichia coli photoreactivating enzyme (PRE) has been purified in large amounts from an E.coli strain lysogenic for a defective lambda bacteriophage carrying the phr gene. The resulting enzyme had a pH optimum of 7.2 and an ionic strength optimum of 0.18. It consisted of an apoprotein and cofactor, both of which were necessary for catalytic activity. The apoprotein had a monomer molecular weight of 35,200 and showed stable aggregates under denaturing conditions. The amino acid analysis of the E.coli enzyme was very similar to that of the photoreactivating enzyme from orchid seedlings (Cattelya aurantiaca). Both had arginine at the amino terminus. The cofactor, like the holoenzyme, showed absorption, magnetic circular dichroism, and emission properties indicative of an adenine moiety. Although the isolated enzyme had an action spectrum which peaked at about 360 nm, neither the cofactor, apoenzyme nor holoenzyme showed any detectable absorption between 300 and 400 nm.}
journal = {Photochem. Photobiol.; (United Kingdom)}
volume = {25:5}
journal type = {AC}
place = {United Kingdom}
year = {1977}
month = {May}
}