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Literature summary for 3.4.23.41 extracted from

  • Cawley, N.X.; Loh, Y.P.
    Yapsin 1 (2004), Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. ), 1, 128-131.
No PubMed abstract available
Search for more literature for 3.4.23.41

Cloned(Commentary)

Cloned (Comment) Organism
gene yps1, DNA and amino acid sequence determination and analysis, expression of recombinant enzyme lacking the GPI-anchor in yeast cells Saccharomyces cerevisiae

Inhibitors

Inhibitors Comment Organism Structure
pepstatin A competitive Saccharomyces cerevisiae
RVSMIKNR peptidomimetic inhibitor Saccharomyces cerevisiae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
60000
-
 x * 60000, non-glycosylated enzyme, 70000-150000, glycosylated enzyme Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Saccharomyces cerevisiae the enzyme is involved in proteolysis of the secretory pathway, regulatory parameters, overview ?
-
 ?
pro-alpha-mating factor + H2O Saccharomyces cerevisiae processing alpha-mating factor + pro-sequence of alpha-mating factor
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein N-linked glycosylation Saccharomyces cerevisiae
proteolytic modification proyapsin 1 processing by autocatalysis, autocatalytic cleavage in a loop structure resulting in two subunits, in vitro activation of the zymogen at pH 4.0 Saccharomyces cerevisiae

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme lacking the GPI-anchor from yeast, purification using inhibitor RVSMIKNR affinity chromatography Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATCH1-39 + H2O good substrate Saccharomyces cerevisiae ?
-
 ?
additional information the enzyme is involved in proteolysis of the secretory pathway, regulatory parameters, overview Saccharomyces cerevisiae ?
-
 ?
additional information the enzyme shows a preference for substrates with basic residues downstream as well as upstream of the scissile bond Saccharomyces cerevisiae ?
-
 ?
pro-alpha-mating factor + H2O processing Saccharomyces cerevisiae alpha-mating factor + pro-sequence of alpha-mating factor
-
 ?
pro-kexin + H2O
-
 Saccharomyces cerevisiae kexin + ?
-
 ?
pro-somatostatin II + H2O processing, cleavage after a single Arg residue Saccharomyces cerevisiae somatostatin-28 + pro-sequence of somatostatin-28
-
 ?

Subunits

Subunits Comment Organism
? x * 60000, non-glycosylated enzyme, 70000-150000, glycosylated enzyme Saccharomyces cerevisiae
More three-dimensional structure determination and analysis Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
More formerly termed yapsin 3, yeast aspartyl protease 3, or Yap3p, the enzyme belongs to the A1 peptidase family Saccharomyces cerevisiae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4 5.5
-
 Saccharomyces cerevisiae

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0001
-
 RVSMIKNR below Saccharomyces cerevisiae
0.0004
-
 pepstatin A
-
 Saccharomyces cerevisiae

pI Value

Organism Comment pI Value Maximum pI Value
Saccharomyces cerevisiae
-
-
 4.5