Deuterolysin

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Deuterolysin
Identifiers
EC no. 3.4.24.39
CAS no. 247028-11-1
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Deuterolysin (EC 3.4.24.39, Penicillium roqueforti protease II, microbial neutral proteinase II, acid metalloproteinase, neutral proteinase II, Penicillium roqueforti metalloproteinase) is an enzyme. [1] [2] [3] [4] [5] This enzyme catalyses the following chemical reaction

Preferential cleavage of bonds with hydrophobic residues in P1'; also Asn3-Gln and Gly8-Ser bonds in insulin B chain

This enzyme is present in Penicillium roqueforti , P. caseicolum , Pyricularia oryzae , Aspergillus sojae and A. oryzae .

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<span class="mw-page-title-main">Glutamic protease</span>

Glutamic proteases are a group of proteolytic enzymes containing a glutamic acid residue within the active site. This type of protease was first described in 2004 and became the sixth catalytic type of protease. Members of this group of protease had been previously assumed to be an aspartate protease, but structural determination showed it to belong to a novel protease family. The first structure of this group of protease was scytalidoglutamic peptidase, the active site of which contains a catalytic dyad, glutamic acid (E) and glutamine (Q), which give rise to the name eqolisin. This group of proteases are found primarily in pathogenic fungi affecting plant and human.

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The sedolisin family of peptidases are a family of serine proteases structurally related to the subtilisin (S8) family. Well-known members of this family include sedolisin ("pseudomonalisin") found in Pseudomonas bacteria, xanthomonalisin ("sedolisin-B"), physarolisin as well as animal tripeptidyl peptidase I. It is also known as sedolysin or serine-carboxyl peptidase. This group of enzymes contains a variation on the catalytic triad: unlike S8 which uses Ser-His-Asp, this group runs on Ser-Glu-Asp, with an additional acidic residue Asp in the oxyanion hole.

References

  1. Nakadai T, Nasuno S, Iguchi N (1973). "Purification and properties of neutral proteinase II from Aspergillus oryzae". Agric. Biol. Chem. 37 (12): 2703–2708. doi: 10.1271/bbb1961.37.2703 .
  2. Gripon JC, Hermier J (1974). "[The proteolytic system of Penicillium roqueforti. III. - Purification, properties and specificity of a protease inhibited by E.D.T.A]". Biochimie. 56 (10): 1323–32. doi:10.1016/s0300-9084(75)80017-4. PMID   4219726.
  3. Sekine H (1976). "Neutral proteinases I and II of Aspergillus sojae action on various substrates". Agric. Biol. Chem. 40 (4): 703–709. doi: 10.1271/bbb1961.40.703 .
  4. Gripon JC, Auberger B, Lenoir J (1980). "Metalloproteases from Penicillium caseicolum and P. roqueforti: comparison of specificity and chemical characterization". The International Journal of Biochemistry. 12 (3): 451–5. doi:10.1016/0020-711x(80)90127-5. PMID   6998789.
  5. Vaganova TI, Ivanova NM, Stepanov VM (1988). "Isolation and properties of the "acid" metalloproteinase from Aspergillus oryzae". Biochemistry (Moscow). 53: 1171–1178.