3.4.23.20: Penicillopepsin

This is an abbreviated version, for detailed information about Penicillopepsin, go to the full flat file.

Reaction

Hydrolysis of proteins with broad specificity similar to that of pepsin A, preferring hydrophobic residues at P1 and P1', but also cleaving Gly20-/-Glu in the B chain of insulin. Clots milk, and activates trypsinogen =

Synonyms

Acid protease A, EC 3.4.23.6, EC 3.4.23.7, mold kinase, More, pencillopepsin-JT1, pencillopepsin-JT2, Penicillium citrinum acid proteinase, Penicillium cyclopium acid proteinase, Penicillium expansum acid proteinase, Penicillium janthinellum acid proteinase, Penicillium janthinellum aspartic proteinase, penicillium kinase, Penicillium roqueforti acid proteinase, penicillopepsin-JT1, penicillopepsin-JT2, penicillopepsin-JT3, Peptidase A, Proteinase, Penicillium aspartic, Proteinase, Penicillium caseicolum aspartic, Proteinase, Penicillium citrinum aspartic, Proteinase, Penicillium cyclopium acid, Proteinase, Penicillium duponti aspartic, Proteinase, Penicillium expansum aspartic, Proteinase, Penicillium janthinellum acid, Proteinase, Penicillium roqueforti aspartic

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.23 Aspartic endopeptidases
                3.4.23.20 Penicillopepsin

Reference

Reference on EC 3.4.23.20 - Penicillopepsin

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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hofmann, T.
Penicillopepsin
Methods Enzymol.
45
434-452
1976
Penicillium janthinellum
Manually annotated by BRENDA team
Emi, S.; Myers, D.V.; Iacobucci, G.A.
Purification and properties of the thermostable acid protease of Penicillium duponti
Biochemistry
15
842-848
1976
Penicillium duponti, Penicillium duponti K 1014
Manually annotated by BRENDA team
Hsu, I.N.; Delbaere, L.T.J.; James, M.N.G.
Penicillopepsin from Penicillium janthinellum crystal structure at 2.8 A and sequence homology with porcine pepsin
Nature
266
140-145
1977
Penicillium janthinellum
Manually annotated by BRENDA team
Hofmann, T.; Allen, B.; Bendiner, M.; Blum, M.; Cunningham, A.
Effect of secondary substrate binding in penicillopepsin: contributions of subsites S3 and S2 to kcat
Biochemistry
27
1140-1146
1988
Penicillium janthinellum
Manually annotated by BRENDA team
Dunn, B.M.; Jimenez, M.; Parten, B.F.; Valler, M.J.; Rolph, C.E.; Kay, J.
A systematic series of synthetic chromophoric substrates for aspartic proteinases
Biochem. J.
237
899-906
1986
Penicillium janthinellum
Manually annotated by BRENDA team
James, M.N.G.; Hsu, I.N.; Delbaere, L.T.J.
Mechanism of acid protease catalysis based on the crystal structure of penicillopepsin
Nature
267
808-813
1977
Penicillium janthinellum
Manually annotated by BRENDA team
Mains, G.; Hofmann, T.
The inactivation of penicillopepsin with 1,2-epoxy-3-(p-nitrophenoxy) propane, an active-site directed reagent
Can. J. Biochem.
52
1018-1023
1974
Penicillium janthinellum
Manually annotated by BRENDA team
Wang, T.T.; Hofmann, T.
Acyl and amino intermediates in penicillopepsin-catalysed reactions and activation by nonsubstrate peptides
Can. J. Biochem.
55
286-294
1977
Penicillium janthinellum
Manually annotated by BRENDA team
Hsu, I.N.; Hofman, T.; Nyburg, S.C.
The crystal structure of penicillopesin at 6 A resolution
Biochem. Biophys. Res. Commun.
72
363-368
1976
Penicillium janthinellum
Manually annotated by BRENDA team
Mabrouk, S.S.; Amr, A.S.; Abdel-Fattah, A.F.
A rennin-like enzyme from Penicillium expansum
Agric. Biol. Chem.
40
419-420
1976
Penicillium expansum
-
Manually annotated by BRENDA team
Hashimoto, H.; Iwaasa, T.; Yokotsuka, T.
Some properties of acid protease from the thermophilic fungus, Penicillium duponti K1014
Appl. Microbiol.
25
578-583
1973
Penicillium duponti, Penicillium duponti K 1014
Manually annotated by BRENDA team
Hashimoto, H.; Kaneko, Y.; Iwaasa, T.; Yokotsuka, T.
Production and purification of acid protease from the thermophilic fungus, Penicillium duponti K1014
Appl. Microbiol.
25
584-588
1973
Penicillium duponti, Penicillium duponti K 1014
Manually annotated by BRENDA team
Blum, M.; Cunningham, A.; Bendiner, M.; Hofmann, T.
Penicillopepsin, the aspartic proteinase from Penicillium janthinellum: substrate-binding effects and intermediates in transpeptidation reactions
Biochem. Soc. Trans.
13
1044-1046
1985
Penicillium janthinellum
Manually annotated by BRENDA team
James, M.N.G.; Sielecki, A.R.
Stereochemical analysis of peptide bond hydrolysis catalyzed by the aspartic proteinase penicillopepsin
Biochemistry
24
3701-3713
1985
Penicillium janthinellum
Manually annotated by BRENDA team
Hofmann, T.; Hodges, R.S.; James, M.N.G.
Effect of pH on the activities of penicillopepsin and Rhizopus pepsin and a proposal for the productive substrate binding mode in penicillopepsin
Biochemistry
23
635-643
1984
Penicillium janthinellum
Manually annotated by BRENDA team
James, M.N.G.; Sielecki, A.R.
Structure and refinement of penicillopepsin at 1.8 A resolution
J. Mol. Biol.
163
299-361
1983
Penicillium janthinellum
Manually annotated by BRENDA team
James, M.N.G.; Sielecki, A.R.; Hayakawa, K.; Gelb, M.H.
Crystallographic analysis of transition state mimics bound to penicillopepsin: difluorostatine- and difluorostatone-containing peptides
Biochemistry
31
3872-3886
1992
Penicillium janthinellum
Manually annotated by BRENDA team
Fraser, M.E.; Strynadka, N.C.J.; Bartlett, P.A.; Hanson, J.E.; James, M.N.G.
Crystallographic analysis of transition-state mimics bound to penicillopepsin: phosphorus-containing peptide analogues
Biochemistry
31
5201-5214
1992
Penicillium janthinellum
Manually annotated by BRENDA team
Houmard, J.; Raymond, M.N.
Further characterization of the Penicillium roqueforti acid protease
Biochimie
61
979-982
1979
Penicillium roqueforti
Manually annotated by BRENDA team
Gripon, J.C.
Inactivation of Penicillium roqueforti acid protease by specific pepsin inhibitors
Biochimie
58
747-749
1976
Penicillium roqueforti
Manually annotated by BRENDA team
Fraser, M.E.; Meyer, J.H.; Bartlett, P.A.; James, M.N.
Overcoming the unfavourable entropic contribution of ligand binding with a macrocyclic inhibitor bound to penicillopepsin
Adv. Exp. Med. Biol.
436
355-359
1998
Penicillium sp.
Manually annotated by BRENDA team
Khan, A.R.; Parrish, J.C.; Fraser, M.E.; Smith, W.W.; Bartlett, P.A.; James, M.N.G.
Lowering the entropic barrier for binding conformationally flexible inhibitors to enzymes
Biochemistry
37
16839-16845
1998
Penicillium janthinellum (P00798)
Manually annotated by BRENDA team
Cao, Q.N.; Stubbs, M.; Ngo, K.Q.; Ward, M.; Cunningham, A.; Pai, E.F.; Tu, G.C.; Hofmann, T.
Penicillopepsin-JT2, a recombinant enzyme from Penicillium janthinellum and the contribution of a hydrogen bond in subsite S3 to k(cat)
Protein Sci.
9
991-1001
2000
Penicillium janthinellum, Penicillium janthinellum NRRL 905
Manually annotated by BRENDA team
Hofmann, T.
Penicillopepsin
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. )
1
99-104
2004
Penicillium camemberti, Penicillium duponti, Penicillium duponti K1014, Penicillium janthinellum (P78735), Penicillium janthinellum, Penicillium janthinellum (Q9HEZ3), Penicillium roqueforti
-
Manually annotated by BRENDA team
Vidossich, P.; Carloni, P.
Binding of phosphinate and phosphonate inhibitors to aspartic proteases: a first-principles study
J. Phys. Chem. B
110
1437-1442
2006
Penicillium janthinellum
Manually annotated by BRENDA team