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Information on EC 3.4.11.21 - aspartyl aminopeptidase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P38821

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.11 Aminopeptidases
                3.4.11.21 aspartyl aminopeptidase
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This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: P38821 not found.
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Word Map
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
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
-
-
aminopeptidase A
-
-
-
-
angiotensinase
-
-
-
-
aspartate aminopeptidase
-
-
-
-
aspartic aminopeptidase
-
-
-
-
aspartyl 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
?
show the reaction diagram
-
-
-
-
?
angiotensin I + H2O
Asp + Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu
show the reaction diagram
-
i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu
-
-
?
angiotensin II + H2O
?
show the reaction diagram
-
-
-
-
?
angiotensin II + H2O
Asp + angiotensin III
show the reaction diagram
-
i.e. Asp-Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe, best substrate
i.e. Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe
-
?
angiotensin II antipeptide + H2O
?
show the reaction diagram
-
-
-
-
?
angiotensin II antipeptide + H2O
Glu + Gly-Val-Thr-Val-His-Pro-Val
show the reaction diagram
-
i.e. Glu-Gly-Val-Thr-Val-His-Pro-Val
-
-
?
angiotensinogen 1-14 + H2O
?
show the reaction diagram
-
-
-
-
?
angiotensinogen 1-14 + H2O
Asp + Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val-Tyr-Ser
show the reaction diagram
-
i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val-Tyr-Ser, low activity
-
-
?
additional information
?
-
-
the enzyme is specific for unblocked N-terminal acidic amino acid residues, no activity with N-acetyl-angiotensinogen 1-14, Tyr-bradykinin, Ile-Ser-bradykinin, and [Sar1, Ala8]-angiotensin II, overview
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
additional information
-
poor inhibition by bestatin at 0.2 mM
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.064
angiotensin I
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
angiotensin I: 100%, angiotensin II: 144%, angiotensinogen 1-14: 35%, angiotensin II antipeptide: 116%, N-acetyl-angiotensinogen 1-14: 0%, Tyr-bradykinin: 0%, Ile-Ser-bradykinin: 0%, [sar1,ala8] angiotensin II: 0%
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
neutral pH-optimum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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a small portion localizes in the vacuole, but its vacuolar transport is accelerated by nutrient starvation, and it stably resides in the vacuole lumen, it is proposed that cytosolic enzyme is redistributed to the vacuole when yeast cells need more active vacuolar degradation
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55000
-
x * 55000, immunoblot analysis
56000
-
monomer, determined by SDS-PAGE
680000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 55000, immunoblot analysis
dodecamer
additional information
-
peptide mass fingerprinting by MALDI-TOF MS analysis
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
aspartyl aminopeptidase is purified from yeast cells, using ultracentrifugation, ammonium sulfate fractionating, and chromatography on a Bio-Gel column, on a Mono Q column, and a Superose 6 column
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native enzyme to homogeneity by ultracentrifugation, ammonium sulfate fractionation, anion exchange chromatography, and gel filtration
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SDS-PAGE, used for immunization
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3), GFP- and hemagglutinin-tagged constructs
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gene YHR113W, located on chromosome VIII, DNA and amino acid sequence determination and analysis
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yokoyama, R.; Kawasaki, H.; Hirano, H.
Identification of yeast aspartyl aminopeptidase gene by purifying and characterizing its product from yeast cells
FEBS J.
273
192-198
2006
Saccharomyces cerevisiae, Saccharomyces cerevisiae B-8032
Manually annotated by BRENDA team
Yuga, M.; Gomi, K.; Klionsky, D.J.; Shintani, T.
Aspartyl aminopeptidase is imported from the cytoplasm to the vacuole by selective autophagy in Saccharomyces cerevisiae
J. Biol. Chem.
286
13704-13713
2011
Saccharomyces cerevisiae
Manually annotated by BRENDA team