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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.4.11.21 - aspartyl aminopeptidase and Organism(s) Schizosaccharomyces pombe and UniProt Accession O36014

for references in articles please use BRENDA:EC3.4.11.21
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.11 Aminopeptidases
                3.4.11.21 aspartyl aminopeptidase
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Schizosaccharomyces pombe
UNIPROT: O36014 not found.
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Schizosaccharomyces pombe
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
release of an N-terminal aspartate or glutamate from a peptide, with a preference for aspartate
Synonyms
aspartyl aminopeptidase, dnpep, aspap, pfm18aap, peptidase e, acid peptidase, tgaap, m18aap, aspartyl-ap, alpha-aspartyl dipeptidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alpha-aspartyl dipeptidase
-
-
-
-
aminopeptidase A
-
-
-
-
angiotensinase
-
-
-
-
aspartate aminopeptidase
-
-
-
-
aspartic aminopeptidase
-
-
-
-
glutamyl aminopeptidase
-
-
-
-
L-aspartate aminopeptidase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
9074-83-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
angiotensin I + H2O
L-Asp + des-Asp-angiotensin I
show the reaction diagram
-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
aspartyl aminopeptidase is a moonlight protein that has aspartyl aminopeptidase and chaperone activities
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
200000
gel filtration
47000
x * 47000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 47000, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE-Sephacel gel filtration and TSK phenyl 5-PW gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lee, S.; Kim, J.S.; Yun, C.H.; Chae, H.Z.; Kim, K.
Aspartyl aminopeptidase of Schizosaccharomyces pombe has a molecular chaperone function
BMB Rep.
42
812-816
2009
Schizosaccharomyces pombe (O36014), Schizosaccharomyces pombe
Manually annotated by BRENDA team