Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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)

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.11.21 47000
-
 x * 47000, SDS-PAGE Schizosaccharomyces pombe
3.4.11.21 200000
-
 gel filtration Schizosaccharomyces pombe

Organism

EC Number Organism UniProt Comment Textmining
3.4.11.21 Schizosaccharomyces pombe O36014
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

EC Number Synonyms Comment Organism
3.4.11.21 AAP
-
 Schizosaccharomyces pombe

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.4.11.21 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

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