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3.4.15.1: peptidyl-dipeptidase A

This is an abbreviated version!
For detailed information about peptidyl-dipeptidase A, go to the full flat file.

Word Map on EC 3.4.15.1

Reaction

release of a C-terminal dipeptide, oligopeptide-/-Xaa-Yaa, when Xaa is not Pro, and Yaa is neither Asp nor Glu. Thus, conversion of angiotensin I to angiotensin II, with increase in vasoconstrictor activity, but no action on angiotensin II =

Synonyms

ACE, ACE-1, ACE2, ACEI, ANCE, ANG I-converting enzyme, angiotensin 1 converting enzyme, angiotensin converting enzyme, angiotensin converting enzyme 1, angiotensin converting enzyme I, angiotensin converting enzyme inhibitor, angiotensin I converting enzyme, angiotensin I-converting enzyme, angiotensin-converting enzyme, angiotensin-converting enzyme 2, angiotensin-converting enzyme type 1, angiotensin-converting enzyme-2, angiotensin-converting-enzyme, angiotensin-I converting enzyme, angiotensin-I-converting enzyme, carboxycathepsin, carboxypeptidase, dipeptidyl, CD143, CD143 antigen, crab-ACE, DCP, Dcp1, Dipeptidyl carboxypeptidase, dipeptidyl carboxypeptidase I, dipeptidylcarboxypeptidase, endothelial cell peptidyl dipeptidase, gACE, germinal ACE, kinases II peptidyldipeptide hydrolase, kininase II, mACE2, More, PDH, peptidase P, peptidyl dipeptidase, peptidyl dipeptidase A, peptidyl dipeptidase I, peptidyl dipeptidase-4, peptidyl dipeptide hydrolase, peptidyl-dipeptide hydrolase, peptidyldipeptide hydrolase, rhACE2, s-ACE, sACE, sACE-1, somatic ACE, somatic angiotensin I-converting enzyme, TACE, testicular ACE, testis ACE, XcACE, zinc dipeptidyl carboxypeptidase, Zn2+ peptidyldipeptidase

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.15 Peptidyl-dipeptidases
                3.4.15.1 peptidyl-dipeptidase A

Posttranslational Modification

Posttranslational Modification on EC 3.4.15.1 - peptidyl-dipeptidase A

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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
phosphoprotein
-
tyrosine phosphorylation of the ectodomain of ACE regulates the cleavage secretion of the enzymatically active ectodomain of angiotensin-converting enzyme. ACE is also phosphorylated at Ser730 of the cytoplasmic domain. Phorbol 12-myristate 13-acetate and calmodulin inhibitor CaMI can enhance both cleavage secretion of ACE and its dephosphorylation
proteolytic modification
sialoglycoprotein
angiotensin-converting enzyme (ACE) is expressed as a type-1 membrane glycoprotein on the surface of endothelial and epithelial cells. Desialylation of ACE is performed by comercial neuraminidase from Vibrio cholerae at pH 6.0, 25°C. While desialylation of seminal fluid ACE does not result in the appearance of any neuraminic acid on the ion-exchange chromatogram, desialylation of lung ACE results in the appearance of 5 neuraminic acid residues per molecule of the enzyme. N-glycosylation sites on the N and C domains of human ACE is analyzed by mass spectrometry, detailed overview. Effect of inactivated human plasma on mAbs binding to two types of ACE differed significantly, with seminal fluid ACE being more sensitive to the presence of plasma. Effect of inactivated seminal fluid on mAbs binding to two types of ACE also showed more prominent effect for seminal fluid ACE, strengthening the suggestion that different conformations of these ACEs can participate in different regulation of the functions of ACEs on endothelial and epithelial cells
side-chain modification