3.4.15.5: Peptidyl-dipeptidase Dcp
This is an abbreviated version!
For detailed information about Peptidyl-dipeptidase Dcp, go to the full flat file.
Word Map on EC 3.4.15.5
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3.4.15.5
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3.4.15.1
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angiotensin
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angiotensin-converting
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captopril
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bradykinin
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i-converting
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dipeptide
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kininase
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endopeptidase
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enkephalin
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3.4.24.11
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enkephalinase
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phosphoramidon
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peptidyldipeptide
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thiorphan
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lisinopril
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enalaprilat
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bestatin
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met5-enkephalin
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hip-his-leu
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amastatin
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dipeptidylaminopeptidase
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metalloendopeptidase
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gly3-phe4
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endopeptidase-24.11
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hippuryl-l-histidyl-l-leucine
- 3.4.15.5
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3.4.15.1
- angiotensin
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angiotensin-converting
- captopril
- bradykinin
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i-converting
- dipeptide
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kininase
- endopeptidase
- enkephalin
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3.4.24.11
- enkephalinase
- phosphoramidon
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peptidyldipeptide
- thiorphan
- lisinopril
- enalaprilat
- bestatin
- met5-enkephalin
- hip-his-leu
- amastatin
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dipeptidylaminopeptidase
- metalloendopeptidase
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gly3-phe4
- endopeptidase-24.11
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hippuryl-l-histidyl-l-leucine
Reaction
Hydrolysis of unblocked, C-terminal dipeptides from oligopeptides, with broad specificity. Does not hydrolyse bonds in which P1' is Pro, or both P1 and P1' are Gly =
Synonyms
DCP, Dipeptidyl carboxypeptidase, dipeptidyl carboxypeptidase II, dipeptidylcarboxypeptidase, EC 3.4.15.1, EC 3.4.15.3, K-26-DCP, LdDCP, More, peptidyl-dipeptidase K-26-DCP
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Substrates Products
Substrates Products on EC 3.4.15.5 - Peptidyl-dipeptidase Dcp
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REACTION DIAGRAM
4-Nitrobenzyloxycarbonyl-Gly-(S-4-nitrobenzo-2-oxa-1,3-diazole)-Cys-Gly + H2O
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angiotensin I + H2O
DRVYIHPF + His-Leu
i.e. DRVYIHPFHL, hydrolysis at the F-H bond generating angiotensin II
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-
?
bradykinin + H2O
RPPGF + Ser-Pro + Phe-Arg
i.e. RPPGFSPFR, hydrolysis at at sequential cleavage sites releasing the C-terminal dipeptides F-R and S-P
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-
?
o-aminobenzoyl-FRAK(2,4-dinitrophenyl)-OH + H2O
o-aminobenzoyl-FR + AK(2,4-dinitrophenyl)-OH
an ACE substrate, Dcp hydrolyzes at the R-A bond
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-
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o-aminobenzoyl-FRK(2,4-dinitrophenyl)P-OH + H2O
o-aminobenzoyl-FR + K(2,4-dinitrophenyl)P-OH
an ACE substrate, Dcp hydrolyzes at the R-K bond
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-
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o-aminobenzoyl-LFK(2,4-dinitrophenyl)-OH + H2O
o-aminobenzoyl-L + FK(2,4-dinitrophenyl)-OH
an ACE substrate, Dcp hydrolyzes at the L-F bond
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-
?
tert-butyloxycarbonyl-Ala-Ala-Ala + H2O
tert-butyloxycarbonyl-Ala + Ala-Ala
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tert-Butyloxycarbonyl-Ala-Glu-Ala-Ala + H2O
tert-Butyloxycarbonyl-Ala-Glu + Ala-Ala
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Acetyl-Ala-Ala-Ala + H2O
Acetyl-Ala + Ala-Ala
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the enzyme is required for the utilization of acetyl-Ala3 as a sole nitrogen source
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Acetyl-Ala3 + H2O
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the enzyme is required for the utilization of acetyl-Ala3 as a sole nitrogen source
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Acetyl-Ala3 + H2O
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the enzyme is required for the utilization of acetyl-Ala3 as a sole nitrogen source
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Benzyloxycarbonyl-Ala + Ala-Ala
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Benzyloxycarbonyl-Ala-Ala-Ala + H2O
Benzyloxycarbonyl-Ala + Ala-Ala
Escherichia coli B / ATCC 11303
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specific cleavage by enzyme K-26-DCP
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human angiotensin I + H2O
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specific cleavage by enzyme K-26-DCP
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the enzyme hydrolyzes the penultimate peptide bond of alpha-N-blocked tripeptides, free tetrapeptides and higher peptides
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additional information
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enzyme requires a free C terminus, and it cannot hydrolyze bonds in which the peptide nitrogen is donated by proline or in which both amino acids are Gly
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additional information
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may have an important function in degradation of intracellular proteins
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additional information
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EcDcp removes dipeptides from the free C-termini of peptides, N-blocked tripeptides and unprotected tetrapeptides
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additional information
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EcDcp removes dipeptides from the free C-termini of peptides, N-blocked tripeptides and unprotected tetrapeptides
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additional information
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no activity with Ac-SDKP-OH, o-aminobenzoyl-FRAK(2,4-dinitrophenyl)-NH2, o-aminobenzoyl-SDK(2,4-dinitrophenyl)P-OH and o-aminobenzoyl-APK(2,4-dinitrophenyl)-OH
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additional information
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no activity with Ac-SDKP-OH, o-aminobenzoyl-FRAK(2,4-dinitrophenyl)-NH2, o-aminobenzoyl-SDK(2,4-dinitrophenyl)P-OH and o-aminobenzoyl-APK(2,4-dinitrophenyl)-OH
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additional information
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Escherichia coli B / ATCC 11303
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the enzyme hydrolyzes the penultimate peptide bond of alpha-N-blocked tripeptides, free tetrapeptides and higher peptides
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?
additional information
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enzyme requires a free C terminus, and it cannot hydrolyze bonds in which the peptide nitrogen is donated by proline or in which both amino acids are Gly
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additional information
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may have an important function in degradation of intracellular proteins
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additional information
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dipeptidylcarboxypeptidase plays a role in parasite nutrition
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additional information
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dipeptidylcarboxypeptidase plays a role in parasite nutrition
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additional information
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enzyme requires a free C terminus, and it cannot hydrolyze bonds in which the peptide nitrogen is donated by proline or in which both amino acids are Gly
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?
additional information
?
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may have an important function in degradation of intracellular proteins
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?