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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

Engineering

Engineering on EC 3.4.11.3 - cystinyl aminopeptidase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A429G
A6909T
naturally occuing mutation, polymorphism A609T interacts with the hinge domain III of IRAP, similarly to SNP K528R in ERAP1, which has been repeatedly validated for disease association and effects on activity. The A609T mutation leads to an almost 2fold reduction in activity compared to wild-type
E431A
-
strong decrease in aminopeptidase activity towards Leu-4-nitroanilide
E431D
-
strong decrease in aminopeptidase activity towards Leu-4-nitroanilide
E465D
-
strong decrease in aminopeptidase activity towards Leu-4-nitroanilide
E465Q
-
strong decrease in aminopeptidase activity towards Leu-4-nitroanilide
E487D
-
strong decrease in aminopeptidase activity towards Leu-4-nitroanilide
E487Q
-
inactive mutant enzyme
G428A
-
the ratio of maximal velocity to Km-value is 90% of the value for the wild-type enzyme
G428D
-
80% of wild-type activity with L-Arg-vasopressin, no activity with L-Leu-enkephalin
G428E
-
50% of wild-type activity with L-Arg-vasopressin, no activity with L-Leu-enkephalin
G428Q
-
more than wild-type activity with L-Arg-vasopressin, less than 10% of wild-type activity with L-Leu-enkephalin
H464Y
-
strong decrease in aminopeptidase activity towards Leu-4-nitroanilide
H468Y
-
strong decrease in aminopeptidase activity towards Leu-4-nitroanilide
I166M
naturally occuing mutation, the I166M polymorphism is located in domain I of the enzyme at the interface with domain II and makes contact with loop 534-538 that is adjacent to the S1 pocket of the enzyme. The mutant enzyme activity is slightly reduced compared to the wild-type
M430E
-
strong decrease in aminopeptidase activity towards Leu-4-nitroanilide
M430I
-
the ratio of maximal velocity to Km-value is 6.2% of the value for the wild-type enzyme
M430K
-
the ratio of maximal velocity to Km-value is 3.3% of the value for the wild-type enzyme
N432A
-
no activity with L-Arg-vasopressin, or L-Leu-enkephalin
C103A/C114A
no effects of mutating the modified cysteines on the plasma membrane localisation of IRAP in transfected HEK-293T cells are detected. Combined mutation of both C103A and C114A leads to a complete loss of IRAP S-acylation
C35A/C103A/C114A
no effects of mutating the modified cysteines on the plasma membrane localisation of IRAP in transfected HEK-293T cells are detected. Combined mutation of both C103A and C114A leads to a complete loss of IRAP S-acylation
L53A/L54A
-
no change in intracellular trafficking
L76A/L77A
-
mutation results in rapid default of the enzyme to the cell surface. In presence of a dominant interfering mutant of clathrin adaptor GGA1, insulin-stimulated translocation of wild-type enzyme, but not of mutant L76A/L77A is inhibited
additional information