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3.4.11.3: cystinyl aminopeptidase

This is an abbreviated version!
For detailed information about cystinyl aminopeptidase, go to the full flat file.

Word Map on EC 3.4.11.3

Reaction

Release of an N-terminal amino acid, Cys-/-Xaa-, in which the half-cystine residue is involved in a disulfide loop, notably in oxytocin or vasopressin. Hydrolysis rates on a range of aminoacyl arylamides exceed that for the cystinyl derivative, however =

Synonyms

alpha-Aminoacyl-peptide hydrolase, aminopeptidase, cystyl, AT4 receptor, CAP, CAP-I, CAP-II, CysAP, cysteine aminopeptidase, cystine aminopeptidase, Cystinyl aminopeptidase, cystinylaminopeptidase, cystyl aminopeptidase, cystyl-aminopeptidase, GP160, insulin regulated aminopeptidase, insulin-regulated aminopeptidase, insulin-regulated aminopeptidase IRAP, Insulin-regulated membrane aminopeptidase, Insulin-responsive aminopeptidase, IRAP, IRAP/P-LAP, L-cystine aminopeptidase, LCAP, LeuAP, leucine aminopeptidase/oxytocinase, leucyl-aminopeptidase, leucyl-cystinyl aminopeptidase, LNPEP, M1 aminopeptidase, OTase, oxytocin peptidase, oxytocinase, oxytocinase/insulin-regulated aminopeptidase, oxytocinase/vasopressinase-like leucyl-cystinyl aminopeptidase LNPEP, P-LAP, P-LAP/IRAP, P-LAP/OTase, placental leucil aminopeptidase, Placental leucine aminopeptidase, placental leucine aminopeptidase/oxytocinase, placental leucine aminopeptidase/oxytocinase/insulin-regulated membrane aminopeptidase, vasopressinase, vasopresssinase, Vesicle protein of 165 kDa, Vp165, yscXVI

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.11 Aminopeptidases
                3.4.11.3 cystinyl aminopeptidase

Posttranslational Modification

Posttranslational Modification on EC 3.4.11.3 - cystinyl aminopeptidase

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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
proteolytic modification
-
the soluble form present in maternal serum is converted from the membrane-bound form in placenta by an enzyme with metalloprotease activity by posttranslational proteolytic cleavage between Phe154 and Ala155
S-acylation
insulin-responsive aminopeptidase (IRAP) is identified as an S-acylated protein in adipocytes and other tissues, semi-quantitative acyl-RAC technique shows that approximately 60% of IRAP is S-acylated in 3T3-L1 adipocytes, palmitoylation. Mapping of the sites of S-acylation on IRAP to two cysteine residues, one of which is predicted to lie in the cytoplasmic side of the single transmembrane domain and the other which is just upstream of this transmembrane domain, these cysteines, C103, and C114, may be modified in a mutually-exclusive manner. Although S-acylation regulates the intracellular trafficking of several transmembrane proteins, no effects of mutating the modified cysteines on the plasma membrane localisation of IRAP in transfected HEK-293T cells are detected, suggesting that S-acylation is not essential for the movement of IRAP through the secretory pathway
side-chain modification