Peptidyl-Lys metalloendopeptidase

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Peptidyl-Lys metalloendopeptidase
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EC no. 3.4.24.20
CAS no. 65979-41-1
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Peptidyl-Lys metalloendopeptidase (EC 3.4.24.20, Armillaria mellea neutral proteinase, peptidyllysine metalloproteinase) is an enzyme. [1] [2] This enzyme catalyses the following chemical reaction

Preferential cleavage in proteins: -Xaa-Lys- (in which Xaa may be Pro)

This enzyme is isolated from the honey fungus Armillaria mellea .

Related Research Articles

<i>Armillaria mellea</i> Species of fungus

Armillaria mellea, commonly known as honey fungus, is a edible basidiomycete fungus in the genus Armillaria. It is a plant pathogen and part of a cryptic species complex of closely related and morphologically similar species. It causes Armillaria root rot in many plant species and produces mushrooms around the base of trees it has infected. The symptoms of infection appear in the crowns of infected trees as discoloured foliage, reduced growth, dieback of the branches and death. The mushrooms are edible but some people may be intolerant to them. This species is capable of producing light via bioluminescence in its mycelium.

Aspergillopepsin I is an enzyme. This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">PPIL2</span> Protein-coding gene in the species Homo sapiens

Peptidyl-prolyl cis-trans isomerase-like 2 is an enzyme that in humans is encoded by the PPIL2 gene.

<span class="mw-page-title-main">Dipeptidyl-peptidase I</span>

Dipeptidyl peptidase I is an enzyme. This enzyme catalyses the following chemical reaction

<i>Armillaria gallica</i> Species of fungus in the family Physalacriaceae

Armillaria gallica is a species of honey mushroom in the family Physalacriaceae of the order Agaricales. The species is a common and ecologically important wood-decay fungus that can live as a saprobe, or as an opportunistic parasite in weakened tree hosts to cause root or butt rot. It is found in temperate regions of Asia, North America, and Europe. The species forms fruit bodies singly or in groups in soil or rotting wood. The fungus has been inadvertently introduced to South Africa. Armillaria gallica has had a confusing taxonomy, due in part to historical difficulties encountered in distinguishing between similar Armillaria species. The fungus received international attention in the early 1990s when an individual colony living in a Michigan forest was reported to cover an area of 15 hectares, weigh at least 9.5 tonnes, and be 1,500 years old. This individual is popularly known as the "humongous fungus", and is a tourist attraction and inspiration for an annual mushroom-themed festival in Crystal Falls. Recent studies have revised the fungus's age to 2,500 years and its size to about 400 tonnes, four times the original estimate.

Lysyl endopeptidase is an enzyme. This enzyme catalyses the following chemical reaction

Adenain is an enzyme. This enzyme catalyses the following chemical reaction

Gingipain K is an enzyme. This enzyme catalyses the following chemical reaction

Mucorpepsin is an enzyme. This enzyme catalyses the following chemical reaction

IgA-specific metalloendopeptidase is an enzyme. This enzyme catalyses the following chemical reaction:

Bacillolysin is an enzyme. This enzyme catalyses the following chemical reaction

Coccolysin is an enzyme. This enzyme catalyses the following chemical reaction

Mycolysin is an enzyme. This enzyme catalyses the following chemical reaction

Beta-lytic metalloendopeptidase is an enzyme. This enzyme catalyses the following chemical reaction

Peptidyl-Asp metalloendopeptidase is an enzyme. This enzyme catalyses the following chemical reaction

Horrilysin is an enzyme. This enzyme catalyses the following chemical reaction

Trimerelysin II is an enzyme. This enzyme catalyses the following chemical reaction

Nardilysin is an enzyme. This enzyme catalyses the following chemical reaction

Flavastacin is an enzyme. This enzyme catalyses the following chemical reaction

References

  1. Doonan S, Doonan HJ, Hanford R, Vernon CA, Walker JM, da Airold LP, et al. (September 1975). "The primary structure of aspartate aminotransferase from pig heart muscle. Digestion with a proteinase having specificity for lysine residues". The Biochemical Journal. 149 (3): 497–506. doi:10.1042/bj1490497d. PMC   1165654 . PMID   1239277.
  2. Lewis WG, Basford JM, Walton PL (February 1978). "Specificity and inhibition studies of Armillaria mellea protease". Biochimica et Biophysica Acta (BBA) - Enzymology. 522 (2): 551–560. doi:10.1016/0005-2744(78)90087-6. PMID   23849.