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Literature summary for 3.4.23.25 extracted from

  • Badasso, M.O.; Read, J.A.; Dhanaraj, V.; Cooper, J.B.; Wood, S.P.; Blundell, T.L.; Dreyer, T.; Winther, J.
    Purification, co-crystallization and preliminary X--ray analysis of the natural aspartic proteinase inhibitor IA3 complexed with saccharopepsin from Saccharomyces cerevisiae (2000), Acta Crystallogr. Sect. D, 56, 915-917.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with natural aspartic proteinase in hibitor IA3, space group P6(2)22, with unit-cell parameters a : b : 192.1 A, c : 59.80 A, native saccharopepsin crystals belongs to the orthorhombic space group I2(1)2(1)2(1) with unit-cell parameters a : 101.4 A, b 0 128.7 A, c : 155.4 A, in complex with CP81,282 and PD130,327 trigonal space group P3(2)21, with unit-cell parameters a 0 b : 87.4 A, c : 110.2 A Saccharomyces cerevisiae

Inhibitors

Inhibitors Comment Organism Structure
CP81,282
-
Saccharomyces cerevisiae
natural aspartic proteinase inhibitor IA3
-
Saccharomyces cerevisiae
natural aspartic proteinase inhibitor IA4
-
Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Saccharomyces cerevisiae 5829
-
vacuole
-
Saccharomyces cerevisiae 5773
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
43000
-
-
Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
baker's yeast
-

Purification (Commentary)

Purification (Comment) Organism
-
Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
Aspartic proteinase
-
Saccharomyces cerevisiae
proteinase-A
-
Saccharomyces cerevisiae
vacuolar aspartic proteinase
-
Saccharomyces cerevisiae