An Introduction to Peptidases and the Merops Database

Rawlings, Neil D.; Morton, Fraser; Barrett, Alan J.

doi:10.1007/1-4020-5377-0_10

Cited by 17 publications

(18 citation statements)

References 32 publications

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“…Proteinases are industrial enzymes widely used for, e.g., milk clotting, meat tenderization, beer clarifying, hair removing in leather industry, manufacture of biological washing powders and contact lens cleaning fluid, medicine (e.g., to remove gastrointestinal parasites and dead skin from burnt patients) or in laboratory work (e.g., protein sequencing, processing of recombinant fusion proteins) (Rawlings et al 2007). Not surprisingly, proteinases account for ≈60 % of total enzyme sales.…”

Section: Ep(s) Extracellular Proteinase(s) Sds-page Sodium Dodecylsulmentioning

confidence: 99%

PepJ is a new extracellular proteinase of Aspergillus nidulans

et al. 2009

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Under carbon starvation, Aspergillus nidulans released a metallo-proteinase with activities comparable to those of PrtA, the major extracellular serine proteinase of the fungus. The relative molar mass of the enzyme was 19 kDa as determined with both denaturing and renaturing SDS PAGE, while its isoelectric point and pH and temperature optima were 8.6, 5.5 and 65 degrees C, respectively. The enzyme was stable at pH 3.5-10.5 and was still active at 95 degrees C in the presence of azocasein substrate. MALDI-TOF MS analysis demonstrated that the proteinase was encoded by the pepJ gene (locus ID AN7962.3), and showed high similarity to deuterolysin from Aspergillus oryzae. The size of the mature enzyme, its EDTA sensitivity and heat stability also supported the view that A. nidulans PepJ is a deuterolysin-type metallo-proteinase.

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Section: Ep(s) Extracellular Proteinase(s) Sds-page Sodium Dodecylsulmentioning

confidence: 99%

PepJ is a new extracellular proteinase of Aspergillus nidulans

et al. 2009

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“…Moreover, the more thermostable enzymes have been found to be resistant to proteolysis and denaturation (Tsai et al, 2001). Approximately 80% of the products obtained from thermophilic organisms used in the industrial field are enzymes, particularly hydrolases, including proteases (Rawlings et al 2007). Protease enzymes are one of the most important industrial enzymes, and different varieties of these enzymes have been used in the food, textile, detergent, leather and pharmaceutical industries (Walsh 2002).…”

Section: Introductionmentioning

confidence: 99%

Extremely Thermostable, Edta-Resistant Alkaline Protease From a Thermophilic Geobacillus Subterraneus C2-1 Isolate

Akkır¹,

Şahin²,

Gedikli³

et al. 2017

J microb biotech food sci

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In this study, the alkaline protease-production capacity of a Geobacillus subterraneus C2-1 isolate from the Çitgöl thermal spring was investigated and optimised using a Plackett-Burman experimental design. In addition to the incubation time, which was the most important parameter, other significant factors were the peptone, glucose, and MgSO4.7H2O concentrations, the activation time and the inoculum amount. The highest protease activity of the Geobacillus subterraneus C2-1 isolate was observed using 14.75 g L-1 glucose as the carbon source, 7.51 g L-1 yeast extract as the nitrogen source, an inoculum amount of 3.56%, a temperature of 56.35 °C, and a reaction time of 168 h. In the presence of 1.0 mM SDS, the protease activity did not change and even increased. Furthermore, 100 mM EDTA yielded a five-fold enhancement in specific activity. The presence of chemical denaturants, chelators, and even heavy metals did not alter the protease activity of the C2-1 isolate.

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“…Almost all of these sequences are derived from genome sequencing projects, often from unusual microbes, and are unlikely to be characterized. Besides their physiological roles, many peptidases have biomedical, scientific and industrial uses (14), and several peptidases from unfamiliar organisms have been used, in cheese-making and biological washing powders, for example. It is thus possible that many of the uncharacterized peptidases will prove to have unique specificities and be equally useful, or at least physiologically interesting.…”

Section: Introductionmentioning

confidence: 99%

Identification and prioritization of novel uncharacterized peptidases for biochemical characterization

Rawlings

2013

Database

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Genome sequencing projects are generating enormous amounts of biological data that require analysis, which in turn identifies genes and proteins that require characterization. Enzymes that act on proteins are especially difficult to characterize because of the time required to distinguish one from another. This is particularly true of peptidases, the enzymes that activate, inactivate and degrade proteins. This article aims to identify clusters of sequences each of which represents the species variants of a single putative peptidase that is widely distributed and is thus merits biochemical characterization.The MEROPS database maintains large collections of sequences, references, substrate cleavage positions and inhibitor interactions of peptidases and their homologues. MEROPS also maintains a hierarchical classification of peptidase homologues, in which sequences are clustered as species variants of a single peptidase; homologous sequences are assembled into a family; and families are clustered into a clan. For each family, an alignment and a phylogenetic tree are generated. By assigning an identifier to a peptidase that has been biochemically characterized from a particular species (called a holotype), the identifier can be automatically extended to sequences from other species that cluster with the holotype. This permits transference of annotation from the holotype to other members of the cluster. By extending this concept to all peptidase homologues (including those of unknown function that have not been characterized) from model organisms representing all the major divisions of cellular life, clusters of sequences representing putative peptidases can also be identified. The 42 most widely distributed of these putative peptidases have been identified and discussed here and are prioritized as ideal candidates for biochemical characterization.Database URL: http://merops.sanger.ac.uk

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An Introduction to Peptidases and the Merops Database

Cited by 17 publications

References 32 publications

PepJ is a new extracellular proteinase of Aspergillus nidulans

PepJ is a new extracellular proteinase of Aspergillus nidulans

Extremely Thermostable, Edta-Resistant Alkaline Protease From a Thermophilic Geobacillus Subterraneus C2-1 Isolate

Identification and prioritization of novel uncharacterized peptidases for biochemical characterization

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