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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

Cloned

Cloned on EC 3.4.15.1 - peptidyl-dipeptidase A

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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a truncated form of mouse ACE2 is cloned into adenovirus vector (Ad-ACE2) and transfected into human THP-1 macrophages
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ACE insertion/deletion genotyping
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AnCE is cloned and expressed in Pichia pastoris
C-catalytic and N-catalytic domain is expressed in CHO cells
expressed as a His-tagged fusion protein in 293F cells
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expressed in 3T3-L1 cells
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expressed in Chinese hamster ovary cells
expression in Chinese hamster ovary cells
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expression in CHO-K1 cells
expression in Escherichia coli strain BL21(DE3)
expression in Pichia pastoris
expression of soluble wild-type and mutant enzymes in CHO and HEK-293 cells
expression of the N-catalytic domain (residues Ala361 to Gly468) of human somatic angiotensin-I converting enzyme in Escherichia coli. The overexpressed protein is exclusively localized to insoluble inclusion bodies
expression of wild-type enzyme and underglycosylated mutant enzymes in CHO cells
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genotyping of ACE insertion and deletion polymorphisms in the Saudi population from Qassim region, genotyping, allele frequencies, overview
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recombinantly expressed
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regions of the testis ACE sequence are replaced with the corresponding N-domain sequence. The resultant chimeras C1-163Ndom-ACE, C417-579Ndom-ACE, and C583-623Ndom-ACE are processed to the cell surface of transfected Chinese hamster ovary cells, and are cleaved at the identical site as that of tACE
somatic enzyme form
stable recombinant expression of ACE in CHO cells and quantitative real-time RT-PCR expression analysis
tissue-specific isozymic forms of angiotensin converting enzyme are encoded by two distinct mRNAs which share sequence homologies
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