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Literature summary for 3.4.11.21 extracted from

  • Lee, S.; Kim, J.S.; Yun, C.H.; Chae, H.Z.; Kim, K.
    Aspartyl aminopeptidase of Schizosaccharomyces pombe has a molecular chaperone function (2009), BMB Rep., 42, 812-816.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Schizosaccharomyces pombe

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
47000
-
x * 47000, SDS-PAGE Schizosaccharomyces pombe
200000
-
gel filtration Schizosaccharomyces pombe

Organism

Organism UniProt Comment Textmining
Schizosaccharomyces pombe O36014
-
-

Purification (Commentary)

Purification (Comment) Organism
DEAE-Sephacel gel filtration and TSK phenyl 5-PW gel filtration Schizosaccharomyces pombe

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
angiotensin I + H2O
-
Schizosaccharomyces pombe L-Asp + des-Asp-angiotensin I
-
?

Subunits

Subunits Comment Organism
? x * 47000, SDS-PAGE Schizosaccharomyces pombe

Synonyms

Synonyms Comment Organism
AAP
-
Schizosaccharomyces pombe

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
60 70 AAP is not precipitated by heat treatment for 30 min at 60°C, only less than 10% of AAP protein is precipitated by heating at 70°C Schizosaccharomyces pombe

General Information

General Information Comment Organism
physiological function aspartyl aminopeptidase is a moonlight protein that has aspartyl aminopeptidase and chaperone activities Schizosaccharomyces pombe