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EC Number
BRENDA No.
Title
Journal
Volume
Pages
Year
Organism
PubMed ID
3.4.23.20
30596
Production and purification of acid protease from the thermophilic fungus, Penicillium duponti K1014
Appl. Microbiol.
25
584-588
1973
Penicillium duponti K 1014
4699218
3.4.23.20
30586
Purification and properties of the thermostable acid protease of Penicillium duponti
Biochemistry
15
842-848
1976
Penicillium duponti
2287
3.4.23.20
30586
Purification and properties of the thermostable acid protease of Penicillium duponti
Biochemistry
15
842-848
1976
Penicillium duponti K 1014
2287
3.4.23.20
30595
Some properties of acid protease from the thermophilic fungus, Penicillium duponti K1014
Appl. Microbiol.
25
578-583
1973
Penicillium duponti
4699217
3.4.23.20
30595
Some properties of acid protease from the thermophilic fungus, Penicillium duponti K1014
Appl. Microbiol.
25
578-583
1973
Penicillium duponti K 1014
4699217
3.4.23.20
30598
Stereochemical analysis of peptide bond hydrolysis catalyzed by the aspartic proteinase penicillopepsin
Biochemistry
24
3701-3713
1985
Penicillium janthinellum
3899173
3.4.23.20
30600
Structure and refinement of penicillopepsin at 1.8 A resolution
J. Mol. Biol.
163
299-361
1983
Penicillium janthinellum
6341600
3.4.23.20
30593
The crystal structure of penicillopesin at 6 A resolution
Biochem. Biophys. Res. Commun.
72
363-368
1976
Penicillium janthinellum
985480
3.4.23.20
30591
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
4609580
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