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Literature summary for 3.4.23.25 extracted from

  • Parr, C.L.; Keates, R.A.; Bryksa, B.C.; Ogawa, M.; Yada, R.Y.
    The structure and function of Saccharomyces cerevisiae proteinase A (2007), Yeast, 24, 467-480.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
1,2-epoxy-3-(p-nitrophenoxy) propane
-
Saccharomyces cerevisiae
CP-108,420
-
Saccharomyces cerevisiae
CP-72,647
-
Saccharomyces cerevisiae
CP-81,198
-
Saccharomyces cerevisiae
CP-81,282
-
Saccharomyces cerevisiae
Diazoacetyl-D,L-norleucine methyl ester
-
Saccharomyces cerevisiae
IA3 peptide inhibitor synthesized by Saccharomyces cerevisae, a synthetic peptide containing residues 2-34 of IA3 exhibits comparable potency to natural IA3 Saccharomyces cerevisiae
PD-129,541
-
Saccharomyces cerevisiae
PD-133,450
-
Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
additional information synthesized as an inactive precursor (zymogen), termed preproPrA, which transits to the endoplasmic reticulum where the protein is glycosylated and a hydrophobic signal peptide of the 22 amino acid is removed, the protein is then transported to the Golgi complex, where the carbohydrate side chains are modified by mannosyltransferases, the resulting 52 kDa proPrA is transported through the endosome to the vacuole, where a 54-amino acid propeptide is removed, yielding the mature 42 kDa proteinase Saccharomyces cerevisiae
-
-
vacuole
-
Saccharomyces cerevisiae 5773
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Saccharomyces cerevisiae essential to the activities of other yeast vacuolar hydrolases, including proteinase B, aminopeptidase I, and carboxypeptidase Y ?
-
?
proproteinase A + H2O Saccharomyces cerevisiae autoactivation of the enzyme yields a functional protein cleaved after Ser68, autoactivation can occur in rare situations when PrB is unable to activate PrA pseudo-proteinaseA + peptide Ser68 is the N-terminal amino acid ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P07267 wild type and proteinase B deficiency strain, in wild-type strains, proPrA is activated to mature PrA with a molecular weight of 42000 Da, whereas in PrB-deficient strains PrA maturation is delayed and a mature pseudo-form of PrA with a molecular weight of 43000 Da is detected
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein glycosylation at Asn67 and Asn266 Saccharomyces cerevisiae

Reaction

Reaction Comment Organism Reaction ID
Hydrolysis of proteins with broad specificity for peptide bonds. Cleaves -Leu-Leu-/-Val-Tyr bond in a synthetic substrate. Does not act on esters of Tyr or Arg description of mechanism, two catalytically active aspartic acid residues, Asp32 and Asp215 Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
A-L-S-A-F-(4NO2)F-R-L + H2O very effective substrate Saccharomyces cerevisiae ?
-
?
A-P-A-K-F-(4NO2)F-R-L + H2O very effective substrate Saccharomyces cerevisiae ?
-
?
K-L-A-K-F-(4NO2)F-R-L + H2O
-
Saccharomyces cerevisiae ?
-
?
K-P-A-A-F-(4NO2)F-R-L + H2O
-
Saccharomyces cerevisiae ?
-
?
K-P-A-K-F-(4NO2)F-R-L + H2O
-
Saccharomyces cerevisiae ?
-
?
K-P-S-K-F-(4NO2)F-R-L + H2O
-
Saccharomyces cerevisiae ?
-
?
additional information essential to the activities of other yeast vacuolar hydrolases, including proteinase B, aminopeptidase I, and carboxypeptidase Y Saccharomyces cerevisiae ?
-
?
additional information preference for hydrophobic residues with Phe, Leu or Glu at the P1 position and Phe, Ile, Leu or Ala at P1’ Saccharomyces cerevisiae ?
-
?
proproteinase A + H2O autoactivation of the enzyme yields a functional protein cleaved after Ser68, autoactivation can occur in rare situations when PrB is unable to activate PrA Saccharomyces cerevisiae pseudo-proteinaseA + peptide Ser68 is the N-terminal amino acid ?

Subunits

Subunits Comment Organism
monomer synthesized as inactive precursor of 405 residues with an apparent molecular weight of 52000 Da, mature nonglycosylated form of PrA has a molecular weight of 35800 Da, mature glycosylated form of PrA has a molecular weight of 41500 Da Saccharomyces cerevisiae
More in PrB-deficient strains PrA maturation is delayed and a mature pseudo-form of PrA with a molecular weight of 43000 Da is detected Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
pepsin-like aspartic proteinase
-
Saccharomyces cerevisiae
PRA
-
Saccharomyces cerevisiae
preproPrA inactive non-glycosylated precursor Saccharomyces cerevisiae
proPrA inactive glycosylated precursor Saccharomyces cerevisiae
Proteinase A
-
Saccharomyces cerevisiae
proteinase A precursor inactive, maturation into active enzyme required proteinase B activity, 405 residues long precursor and 329 residues for the mature protein (77-405) Saccharomyces cerevisiae
pseudo-proteinase A active form of the enzyme resulting from autoactivation Saccharomyces cerevisiae