Comparative biochemistry of the proteinases of eucaryotic microorganisms.
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This article is published in Microbiological Research.The article was published on 1982-09-01 and is currently open access. It has received 289 citations till now. The article focuses on the topics: Comparative Biochemistry.read more
Citations
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Journal ArticleDOI
Molecular and Biotechnological Aspects of Microbial Proteases
TL;DR: Despite the extensive research on several aspects of proteases, there is a paucity of knowledge about the roles that govern the diverse specificity of these enzymes and deciphering these secrets would enable to exploit proteases for their applications in biotechnology.
Journal ArticleDOI
Clinical and Microbiological Aspects of Trichomonas vaginalis
TL;DR: These studies have illustrated that the pathogenesis of T. vaginalis is indeed very complex and involves adhesion, hemolysis, and soluble factors such as cysteine proteinases and cell-detaching factor, and certain stress responses enable the organism to survive in its changing environment.
Journal ArticleDOI
Enzymatic pathway for the bacterial degradation of the cyanobacterial cyclic peptide toxin microcystin LR.
David G. Bourne,Gary J. Jones,Robert L. Blakeley,Alun Jones,Andrew P. Negri,Peter W. Riddles +5 more
TL;DR: An isolated bacterium, identified as a new Sphingomonas species, was demonstrated to contain a novel enzymatic pathway which acted on microcystin LR, the most common cyanobacterial cyclic peptide toxin, and were nontoxic to mice at doses up to 250 micrograms/kg.
Book ChapterDOI
Nitrogen catabolite repression in yeasts and filamentous fungi.
Wiame Jm,Grenson M,Arst Hn +2 more
TL;DR: A brief description of nitrogen catabolite repression in Saccharomyces cerevisiae is provided and a mechanism, nitrogen metabolite repression of the syntheses of many enzymes and permeases involved in nitrogen nutrition, has been extensively studied in two filamentous fungi.
Journal ArticleDOI
Characterisation of a gene cluster involved in bacterial degradation of the cyanobacterial toxin microcystin LR
TL;DR: It is postulated on the basis of comparison with other microorganisms that the genes in this cluster may all be involved in cell wall peptidoglycan cycling and subsequently act fortuitously in hydrolysis of microcystin LR.
References
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Journal ArticleDOI
On the size of the active site in proteases. I. Papain.
Israel Schechter,Arieh Berger +1 more
Journal ArticleDOI
Transfer of Proteins Across Membranes
TL;DR: This paper presents a meta-analysis of the structure of Signal Peptides and their interaction with Membrane, and investigates the role of Ribosome Binding and Translocation of Polypeptide Chains in Peptidase activity.
Journal ArticleDOI
Proteinase K from Tritirachium album Limber
Wolfgang Dr Ebeling,Norbert Dr Hennrich,Michael Dr Klockow,Harald Dr. Metz,Hans Dieter Orth,H. Lang +5 more
TL;DR: The nucleotide-sequence analysis of the gene and its flanking regions has revealed that the proteinase-K gene is composed of two exons and one 63-bp-long intron located in the proregion, and a putative promoter sequence and a capping site have been identified, suggesting that the transcription-start site is located 103-bp upstream of the ATG initiation codon.
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Proteinase mutants of Saccharomyces cerevisiae.
TL;DR: Fifty-nine mutants with reduced ability to cleave the chymotrypsin substrate N-acetyl-DL-phenylalanine beta-naphthyl ester have been isolated in S. cerevisiae and these mutations define 16 complementation groups.
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Structural evidence for gene duplication in the evolution of the acid proteases.
TL;DR: X-ray studies of acid proteases indicate a bilobal structure with a well defined active site cleft and a possible mechanism for evolution by gene duplication, divergence and gene fusion is presented.