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Literature summary for 3.4.11.7 extracted from

  • Rozenfeld, R.; Muller, L.; El Messari, S.; Llorens-Cortes, C.
    The C-terminal domain of aminopeptidase A is an intramolecular chaperone required for the correct folding, cell surface expression, and activity of this monozinc aminopeptidase (2004), J. Biol. Chem., 279, 43285-43295.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of His-tagged or FLAG-tagged wild-type enzyme, and of isolated His- or FLAG-tagged N-terminal, and HA-tagged C-terminal domain in CHO-K1 cells and AtT-20 cells, expression in trans of the separate C- and N-terminal domains rescues enzyme functions, overview Mus musculus

Inhibitors

Inhibitors Comment Organism Structure
glutamate phosphonic acid
-
Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane integral, cell surface Mus musculus 16020
-
additional information deletion of the C-terminal domain abolishes the maturation and enzymatic activity of the N-terminal domain, which remains in the endoplasmic reticulum bound to calnexin as unfolded protein Mus musculus
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ activates Mus musculus
Zn2+ monozinc aminopeptidase, binds to the catalytic site Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
angiotensin II + H2O Mus musculus the enzyme is responsible for the convertion of angiotensin II into angiotensin III in the brain Asp + angiotensin III
-
?
additional information Mus musculus The C-terminal domain of aminopeptidase A is an intramolecular chaperone required for the correct folding, cell surface expression, and activity of the enzyme ?
-
?

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein
-
Mus musculus
additional information enzyme maturation, folding, and trafficking, overview Mus musculus
proteolytic modification the enzyme's ectodomain is cleaved in the kidney in to an N-terminal fragment, corresponding to the zinc metallopeptidase domain, and a C-terminal fragment Mus musculus

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
Mus musculus
-
kidney the enzyme's ectodomain is cleaved in the kidney in to an N-terminal fragment, corresponding to the zinc metallopeptidase domain, and a C-terminal fragment Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
angiotensin II + H2O i.e. Asp-Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe Mus musculus Asp + angiotensin III i.e. Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe ?
angiotensin II + H2O the enzyme is responsible for the convertion of angiotensin II into angiotensin III in the brain Mus musculus Asp + angiotensin III
-
?
additional information The C-terminal domain of aminopeptidase A is an intramolecular chaperone required for the correct folding, cell surface expression, and activity of the enzyme Mus musculus ?
-
?
N-(alpha-L-glutamyl)-4-nitroanilide + H2O
-
Mus musculus L-glutamic acid + 4-nitroaniline
-
?

Subunits

Subunits Comment Organism
More the C-terminal domain is required for enzyme maturation, N-terminal domain activation, and cell surface localization, deletion of the C-terminal domain abolishes the maturation and enzymatic activity of the N-terminal domain, which remains in the endoplasmic reticulum bound to calnexin as unfolded protein Mus musculus

Synonyms

Synonyms Comment Organism
aminopeptidase A
-
Mus musculus
APA
-
Mus musculus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Mus musculus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
assay at Mus musculus