Literature summary for 3.4.16.5 extracted from

Shin, S.Y.; Bae, Y.H.; Kim, S.K.; Seong, Y.J.; Choi, S.H.; Kim, K.H.; Park, Y.C.; Seo, J.H.
Effects of signal sequences and folding accessory proteins on extracellular expression of carboxypeptidase Y in recombinant Saccharomyces cerevisiae (2014), Bioprocess Biosyst. Eng., 37, 1065-1071.

Search for more literature for 3.4.16.5

Activating Compound

Activating Compound	Comment	Organism	Structure
Kar2p, Pdi1p, Ero1p	co-expression of Kar2p, Pdi1p and Ero1p give a synergistic effect on CPY expression, of which activity is 1.7times higher than that of the control strain	Saccharomyces cerevisiae
Karp2	a single co-expression of Kar2p leads to a 28% enhancement in extracellular CPY activity, relative to the control strain	Saccharomyces cerevisiae

Cloned(Commentary)

Cloned (Comment)	Organism
three signal sequences of Saccharomyces cerevisiae mating factor a (MFalpha) and invertase (SUC2), and Kluyveromyces marxianus inulinase (INU1) are combined with proCPY to increase a transporting efficiency from the endoplasmic reticulum in Saccharomyces cerevisiae. The MFalpha signal sequence gives the best specific activity of extracellular CPY	Saccharomyces cerevisiae

Protein Variants

Protein Variants	Comment	Organism
additional information	three signal sequences of Saccharomyces cerevisiae mating factor a (MFalpha) and invertase (SUC2), and Kluyveromyces marxianus inulinase (INU1) are combined with proCPY to increase a transporting efficiency from the endoplasmic reticulum in Saccharomyces cerevisiae. The MFalpha signal sequence gives the best specific activity of extracellular CPY	Saccharomyces cerevisiae

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	-	-	-

Synonyms

Synonyms	Comment	Organism
carboxypeptidase Y	-	Saccharomyces cerevisiae
proCPY	-	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)