Comparative biochemistry of the proteinases of eucaryotic microorganisms.

North, Michael

doi:10.1128/mmbr.46.3.308-340.1982

Cited by 196 publications

(70 citation statements)

References 180 publications

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“…From these results it appears clear that an alkaline (probably serine) protease released from A. persicinum in neutral or alkaline culture conditions is responsible for the inactivation of GNI and the subsequent inability to detect this enzyme under these conditions. Similar in vivo proteolytic inactivation of extracellular enzymes has been reported frequently in fungi [ 15,19,20]. However, a search of the literature failed to find any other reports providing direct evidence for this with extracellular fungal (1 + 3)-p-glucanases, although some studies have implied that it may occur [21-231. These results emphasise the care needed to avoid possible misinterpretation of data gained on the synthesis and regulation of extracellular P-glucanases where such proteolytic activity may interfere.…”

Section: Inhibitor Addedsupporting

confidence: 52%

“…Further differences in the crude protease preparations from acidic and alkaline media were also apparent when they were exposed to known protease inhibitors (Table 3). Phenylmethylsulfonyl fluoride (PMSF) almost totally inhibited the activity of the 'alkaline protease', but only partially inhibited the 'acid protease', indicating the presence of serine proteases [15], although PMSF is also known to inhibit some cysteine proteases [17]. The remaining activity in the 'acid protease' preparation was probably due to aspartic proteases, since the activity was highest at low pH (Fig.…”

Section: A Persicinummentioning

confidence: 99%

“…The remaining activity in the 'acid protease' preparation was probably due to aspartic proteases, since the activity was highest at low pH (Fig. 2) [15]. Therefore, some differences in the proteolytic activity produced under acidic and alkaline conditions clearly exist, although it is not yet known if these enzymes are actively secreted or simply intracellular enzymes released through cell autolysis under these conditions [ 181.…”

Section: A Persicinummentioning

confidence: 99%

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Proteolytic inactivation of an extracellular (1 → 3)-β-glucanase from the fungus Acremonium persicinum is associated with growth at neutral or alkaline medium pH

Pitson¹

1996

FEMS Microbiology Letters

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The filamentous fungus Acremonium persicinum released high levels of proteolytic enzyme activity into the culture fluid during growth at pH 7 or above. Almost total inhibition of this crude activity by phenylmethylsulfonyl fluoride suggested that it was mainly due to the presence of a serine protease. This protease inactivated one of three extracellular (1-->3)-beta-glucanases produced by this fungus, although the activities of the remaining two (1-->3)-beta-glucanases did not appear to be affected. Growth of A. persicinum in acidic conditions resulted in the presence of much lower extracellular proteolytic activity and no apparent (1-->3)-beta-glucanase inactivation.

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Section: Inhibitor Addedsupporting

confidence: 52%

Section: A Persicinummentioning

confidence: 99%

Section: A Persicinummentioning

confidence: 99%

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Proteolytic inactivation of an extracellular (1 → 3)-β-glucanase from the fungus Acremonium persicinum is associated with growth at neutral or alkaline medium pH

Pitson¹

1996

FEMS Microbiology Letters

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“…The nearly exponential increase in summaries and reviews on this topic in the past years probably demonstrates best the rapid progression in this field. Only a selection of the literature can be given here [1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16][17][18][19][20].…”

Section: Introductionmentioning

confidence: 99%

Proteinase function in yeast: Biochemical and genetic approaches to a central mechanism of post-translational control in the eukaryote cell

Rendueles

1988

FEMS Microbiology Letters

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“…There are four different classes of proteinases: aspartic, cysteine, metallo and serine which differ in their in vitro properties. The class to which a specific proteinase belongs is determined by the pH range over which it is active, by its ability to hydrolyze specific proteins, by its similarity to well characterized proteinases and by its sensitivity to various inhibitors (North, 1982). The digestive proteinases of relatively few insect species have been characterized.…”

Section: Introductionmentioning

confidence: 99%

Suppression of larval Colorado potato beetle growth and development by digestive proteinase inhibitors

Wolfson¹,

Murdock²

1987

Entomologia Exp Applicata

101

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Evidence is presented that the Colorado potato beetle (CPB) (Leptinotarsa decemlineata (Say)) depends, at least partially, on cysteine proteinases for protein digestion. Midgut homogenates of CPB larvae have a mildly acidic pH and exhibit major proteolytic activity in the mildly acidic pH range. This proteolytic activity is activated by reducing agents, is inhibited by E‐64 (a specific cysteine proteinase inhibitor), and is not inhibited by serine proteinase inhibitors. In addition, consumption of E‐64 treated potato leaves by CPB larvae at rates as low as 0.8 μg/cm2 of leaf tissue has a deleterious effect on larval growth and development. Résumé Suppression par des inhibiteurs de protéinases intestinales, de la croissance et du développement des larves de doryphores Les protéinases intestinales des larves de Leptinotarsa decemlineata sont en partie caractérisées par les pH limitant leur activité, et par l'effet d'inhibiteurs de protéinases de spécificités connues. Les protéinases ont été testées avec la méthémoglobine tritiée comme substrat et nous avons déterminé les taux relatifs de peptides radioactives TCA solubles, libérées, dans des conditions précises, pour des pH compris entre 2,0 et 12,0. Le taux le plus élevé d'activité protéolytique a été observé pour des pH 5,0 à 6,0, bien qu'il y ait eu une activité appréciable aux pH 4,0 et 8,0. Parmi les inhibiteurs examinés, le E‐64, inhibiteur protéinase cystéine très sélectif, a été le plus efficace sur l'activité protéinase. La pepstatine, inhibiteur protéinase aspartique, a été actif, mais seulement dans une gamme plus moin de pH. Les inhibiteurs protéinase sérine, ont été pratiquement inactifs sur l'activité protéinase. Chez des larves de doryphores nourries de feuilles de pommes de terre traitées avec différentes concentrations de E‐64 ou de pepstatine, la consommation de E‐64 a retardé fortement la croissance larvaire et le développement, la pepstatine a provoqué un retard du développement plus limitée. Nos résultats suggèrent que le doryphore dépend, tout au moins partiellement, des protéinases cystéine pour l'assimilation des protéines.

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Comparative biochemistry of the proteinases of eucaryotic microorganisms.

Cited by 196 publications

References 180 publications

Proteolytic inactivation of an extracellular (1 → 3)-β-glucanase from the fungus Acremonium persicinum is associated with growth at neutral or alkaline medium pH

Proteolytic inactivation of an extracellular (1 → 3)-β-glucanase from the fungus Acremonium persicinum is associated with growth at neutral or alkaline medium pH

Proteinase function in yeast: Biochemical and genetic approaches to a central mechanism of post-translational control in the eukaryote cell

Suppression of larval Colorado potato beetle growth and development by digestive proteinase inhibitors

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