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Involvement of an endogenous metalloprotease in the activation of protoxin in Bacillus thuringiensis subsp. kurstaki.
Biochem Mol Biol Int. 1997 Aug; 42(5):901-8.BM

Abstract

Insecticidal crystal proteins harvested from sporulated cultures of Bacillus thuringiensis subsp. kurstaki contain the protoxin (Mr 132 kDa) and minor amounts of toxin (66 kDa). The proteolytic processing of 132 kDa protoxin to an active 66 kDa toxin is brought about by exogenous proteases or larval gut enzymes. Under denaturing/reducing conditions this conversion is also mediated by endogenous protease(s) of the producer organism. This endogenous protease is identified as a metalloprotease as the activation process is inhibited by ethylenediamine tetraacetic acid at 2 mM concentration.

Authors+Show Affiliations

Kumar NS
Department of Biochemistry, Osmania University, Hyderabad, India.
Venkateswerlu G
No affiliation info available

MeSH

Bacillus thuringiensisBacterial ProteinsBacterial ToxinsInsecticidesMetalloendopeptidasesProtein Precursors

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

9285057

Citation

Kumar, N S., and G Venkateswerlu. "Involvement of an Endogenous Metalloprotease in the Activation of Protoxin in Bacillus Thuringiensis Subsp. Kurstaki." Biochemistry and Molecular Biology International, vol. 42, no. 5, 1997, pp. 901-8.
Kumar NS, Venkateswerlu G. Involvement of an endogenous metalloprotease in the activation of protoxin in Bacillus thuringiensis subsp. kurstaki. Biochem Mol Biol Int. 1997;42(5):901-8.
Kumar, N. S., & Venkateswerlu, G. (1997). Involvement of an endogenous metalloprotease in the activation of protoxin in Bacillus thuringiensis subsp. kurstaki. Biochemistry and Molecular Biology International, 42(5), 901-8.
Kumar NS, Venkateswerlu G. Involvement of an Endogenous Metalloprotease in the Activation of Protoxin in Bacillus Thuringiensis Subsp. Kurstaki. Biochem Mol Biol Int. 1997;42(5):901-8. PubMed PMID: 9285057.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Involvement of an endogenous metalloprotease in the activation of protoxin in Bacillus thuringiensis subsp. kurstaki. AU - Kumar,N S, AU - Venkateswerlu,G, PY - 1997/8/1/pubmed PY - 1997/8/1/medline PY - 1997/8/1/entrez SP - 901 EP - 8 JF - Biochemistry and molecular biology international JO - Biochem Mol Biol Int VL - 42 IS - 5 N2 - Insecticidal crystal proteins harvested from sporulated cultures of Bacillus thuringiensis subsp. kurstaki contain the protoxin (Mr 132 kDa) and minor amounts of toxin (66 kDa). The proteolytic processing of 132 kDa protoxin to an active 66 kDa toxin is brought about by exogenous proteases or larval gut enzymes. Under denaturing/reducing conditions this conversion is also mediated by endogenous protease(s) of the producer organism. This endogenous protease is identified as a metalloprotease as the activation process is inhibited by ethylenediamine tetraacetic acid at 2 mM concentration. SN - 1039-9712 UR - https://www.unboundmedicine.com/medline/citation/9285057/Involvement_of_an_endogenous_metalloprotease_in_the_activation_of_protoxin_in_Bacillus_thuringiensis_subsp__kurstaki_ DB - PRIME DP - Unbound Medicine ER -