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EC Tree
The expected taxonomic range for this enzyme is: Bos taurus
Reaction Schemes
release of a C-terminal dipeptide or exceptionally a tripeptide
Synonyms
Atrial di-(tri-)peptidyl carboxyhydrolase, Atrial dipeptidyl carboxyhydrolase, Atrial peptide convertase, Atriopeptin convertase, Dipeptidase, peptidyl-, B, Dipeptidyl carboxyhydrolase,
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Atrial di-(tri-)peptidyl carboxyhydrolase
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Atrial dipeptidyl carboxyhydrolase
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Atrial peptide convertase
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Atriopeptin convertase
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Dipeptidase, peptidyl-, B
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Dipeptidyl carboxyhydrolase
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release of a C-terminal dipeptide or exceptionally a tripeptide
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hydrolysis of peptide bond
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-
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2-aminobenzoyl-Gly-Ala-(4-nitro)Phe-Arg + H2O
2-aminobenzoyl-Gly-Ala + 4-nitro-L-phenylalanyl-L-arginine
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-
-
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?
2-aminobenzoyl-Gly-Asn-(4-nitro)Phe-Arg + H2O
2-aminobenzoyl-Gly-Asn + 4-nitro-L-phenylalanyl-L-arginine
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-
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?
2-aminobenzoyl-Gly-Asp-(4-nitro)Phe-Arg + H2O
2-aminobenzoyl-Gly-Asp + 4-nitro-L-phenylalanyl-L-arginine
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-
-
-
?
2-aminobenzoyl-Gly-Lys-(4-nitro)Phe-Arg + H2O
2-aminobenzoyl-Gly-Lys + 4-nitro-L-phenylalanyl-L-arginine
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-
-
-
?
2-aminobenzoyl-Gly-Ser-(4-nitro)Phe-Arg + H2O
2-aminobenzoyl-Gly-Ser + 4-nitro-L-phenylalanyl-L-arginine
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-
-
-
?
2-aminobenzoyl-Gly-Thr-(4-nitro)Phe-Arg + H2O
2-aminobenzoyl-Gly-Thr + 4-nitro-L-phenylalanyl-L-arginine
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?
Atriopeptin II + H2O
Atriopeptin I + ?
Atriopeptin II peptide Ser103-Arg125 + H2O
Atriopeptin I peptide Ser103-Ser123 + Phe-Arg
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-
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?
Atriopeptin III peptide Ser103-Tyr126 + H2O
Atriopeptin I + Phe-Arg-Tyr
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?
Benzoyl-Asn-Ser-Phe-Arg-Tyr + H2O
Benzoyl-Asn-Ser-Phe + Arg-Tyr
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successive dipeptidyl cleavage after longer incubation yielding benzoyl-Asn + Ser-Phe
?
Benzoyl-Gly-Asn-Ser + H2O
?
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?
benzoyl-Gly-Gly-Phe-Arg + H2O
benzoyl-Gly-Gly + Phe-Arg
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?
benzoyl-Gly-His-Gly + H2O
benzoyl-Gly + His-Gly
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?
benzoyl-Gly-His-Leu + H2O
?
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?
Benzoyl-Gly-Phe-Ser-Arg + H2O
?
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?
benzoyl-Gly-Ser-Phe-Arg + H2O
benzoyl-Gly-Ser + Phe-Arg
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?
[Mercaptopropionyl105,(D)Ala107]-atriopeptinIII-NH2 peptide + H2O
Analog(1-18) + Phe-Arg-Tyr-NH2
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enzyme acts exclusively as tripeptidyl carboxyhydrolase
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?
additional information
?
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Atriopeptin II + H2O
Atriopeptin I + ?
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?
Atriopeptin II + H2O
Atriopeptin I + ?
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atriopepin I is not a substrate
sequential cleavage of Asn-Ser does not occur, ? is Phe-Arg
?
additional information
?
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generally restricted to the release of dipeptides. In contrast to peptidyl-dipeptidase A (EC 3.4.15.1) it shows no action on angiotensin I. Conversely, peptidyl-dipeptidase A is unable to release Phe-Arg from the C-terminus of atriopeptin II
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?
additional information
?
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not: benzoyl-Asn-Ser-Phe-Arg-Tyr-NH2
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?
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additional information
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in contrast to peptidyl-dipeptidase A (EC 3.4.15.1) it displays no dependence on Cl-
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2-D-Methylsuccinyl-L-Pro
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3-Mercaptopropanoyl-L-Pro
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Benzoyl-Asn-Ser-Phe-Arg-Tyr-NH2
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competitive inhibitor of 2-aminobenzoyl-Gly-Ala-Phe(4-nitro)-Arg hydrolysis and benzoyl-Asn-Ser-Phe-Arg-Tyr hydrolysis
bradykinin potentiating factor
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D-2-Methyl-3-mercaptopropanoyl-L-Pro
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i.e. captopril
additional information
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marked substrate inhibition with benzoyl-Gly-His-Leu, but little or no substrate inhibition with benzoyl-Gly-His-Gly; the enzyme is 5500 times less sensitive to D-Cys-L-Pro, the very potent inhibitor of angiotensin I-converting enzyme (EC 3.4.15.1)
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EDTA
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EDTA
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activity is restored by addition of Co2+, Zn2+ and Mn2+, but not by Cu2+, Mg2+, Ca2+ or Cd2+
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0.102
2-Aminobenzoyl-Gly-Ala-(4-nitro)Phe-Arg
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0.09 - 0.213
2-Aminobenzoyl-Gly-Asp-(4-nitro)Phe-Arg
0.129
2-Aminobenzoyl-Gly-Lys-(4-nitro)Phe-Arg
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-
0.14
2-Aminobenzoyl-Gly-Ser-(4-nitro)Phe-Arg
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0.1
2-Aminobenzoyl-Gly-Thr-(4-nitro)Phe-Arg
0.124 - 0.27
Atriopeptin I
1.13
benzoyl-Gly-Gly-Phe-Arg
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2.4
benzoyl-Gly-His-Gly
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0.8
benzoyl-Gly-His-Leu
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0.12
benzoyl-Gly-Ser-Phe-Arg
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0.09
2-Aminobenzoyl-Gly-Asp-(4-nitro)Phe-Arg
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0.213
2-Aminobenzoyl-Gly-Asp-(4-nitro)Phe-Arg
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0.1
2-Aminobenzoyl-Gly-Thr-(4-nitro)Phe-Arg
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0.1
2-Aminobenzoyl-Gly-Thr-(4-nitro)Phe-Arg
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[mercaptopropionyl105,(D)Ala107]-atriopeptin III-NH2
0.124
Atriopeptin I
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additional information
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6.5 - 9
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6.5: about 65% of activity maximum, 9: about 60% of activity maximum
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brenda
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brenda
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brenda
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240000
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bovine, sucrose density gradient sedimentation, gel filtration
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Harris, R.B.; Wilson, I.B.
Atrial tissue contains a metallo dipeptidyl carboxyhydrolase not present in ventricular tissue: partial purification and characterization
Arch. Biochem. Biophys.
233
667-675
1984
Bos taurus
brenda
Soler, D.F.; Harris, R.B.
Continuous fluorogenic substrates for atrial dipeptidyl carboxyhydrolase. Importance of Ser in the P1 position
Int. J. Pept. Protein Res.
32
35-40
1988
Bos taurus
brenda
Harris, R.B.; Wilson, I.B.
Conversion of atriopeptin II to atriopeptin I by atrial dipeptidyl carboxy hydrolase
Peptides
6
393-396
1985
Bos taurus
brenda
Soler, D.F.; Harris, R.B.
Atrial dipeptidyl carboxyhydrolase is a zinc-metallo proteinase which possesses tripeptidyl carboxyhydrolase activity
Peptides
10
63-68
1989
Bos taurus
brenda
Barrett, A.J.
Peptidyl-dipeptidase B
Handbook of proteolytic enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds. ) Academic Press
1
1029-1030
2004
Bos taurus
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brenda
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3.4.15.4 Peptidyl-dipeptidase B
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