Mucorpepsin

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Mucorpepsin
Identifiers
EC no.3.4.23.23
CAS no.148465-73-0
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
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NCBIproteins

Mucorpepsin (EC 3.4.23.23, Mucor rennin, Mucor aspartic proteinase, Mucor acid proteinase, Mucor acid protease, Mucor miehei aspartic proteinase, Mucor miehei aspartic protease, Mucor pusillus emporase, Fromase 100, Mucor pusillus rennin, Fromase 46TL, Mucor miehei rennin) is an enzyme .[1][2][3][4][5] This enzyme catalyses the following chemical reaction

Hydrolysis of proteins, favouring hydrophobic residues at P1 and P1'. Clots milk. Does not accept Lys at P1, and hence does not activate trypsinogen

This enzyme is isolated from the zygomycete fungi Mucor pusillus and M. miehei.

References

  1. ^ Arima K, Yu J, Iwasaki S (1970). "Milk-clotting enzyme from Mucor pusillus var. lindt". Methods Enzymol. 19: 446–459. doi:10.1016/0076-6879(70)19033-1.
  2. ^ Ottesen M, Rickert W (1970). "The acid protease of Mucor miehei". Methods Enzymol. 19: 459–460. doi:10.1016/0076-6879(70)19034-3.
  3. ^ Sternberg M (December 1972). "Bond specificity, active site and milk clotting mechanism of the Mucor miehei protease". Biochimica et Biophysica Acta (BBA) - Protein Structure. 285 (2): 383–92. doi:10.1016/0005-2795(72)90324-8. PMID 4573298.
  4. ^ Oka T, Ishino K, Tsuzuki H, Morihara K, Arima K (1973). "On the specificity of a rennin-like enzyme from Mucor pusillus". Agric. Biol. Chem. 37 (5): 1177–1184. doi:10.1271/bbb1961.37.1177.
  5. ^ Baudys M, Foundling S, Pavlík M, Blundell T, Kostka V (August 1988). "Protein chemical characterization of Mucor pusillus aspartic proteinase. Amino acid sequence homology with the other aspartic proteinases, disulfide bond arrangement and site of carbohydrate attachment". FEBS Letters. 235 (1–2): 271–4. doi:10.1016/0014-5793(88)81277-8. PMID 3042459.

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