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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

Metals Ions

Metals Ions on EC 3.4.15.1 - peptidyl-dipeptidase A

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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CaCl2
-
activates in absence of Cl-, maximal activity at 0.3 mM
Cl-
-
the activity of the C-domain of sACE depends highly on chloride ion concentration and is inactive in its absence, whereas the N-domain can be completely activated at relatively low concentrations of this anion and is still active in the absence of chloride
CoCl2
-
0.1-1.0 mM, 2fold activation
KBr
-
activation is lower than with NaCl
KI
-
activation is lower than with NaCl
Mn2+
activates, but to a lesser extent than Zn2+
Na2SO4
-
activates in absence of Cl-
NaF
-
activation is lower than with NaCl
additional information
-
enzyme is not affected by addition of 0.1-1.0 mM CaCl2, Mn2Cl2, MgCl2 or 0.1 mM ZnCl2