3.4.14.4: dipeptidyl-peptidase III
This is an abbreviated version!
For detailed information about dipeptidyl-peptidase III, go to the full flat file.
Word Map on EC 3.4.14.4
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3.4.14.4
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exopeptidase
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tynorphin
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enkephalin-degrading
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leu-enkephalin
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nudix
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spinorphin
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hexxh
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map2k5
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medicine
- 3.4.14.4
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exopeptidase
- tynorphin
-
enkephalin-degrading
- leu-enkephalin
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nudix
- spinorphin
-
hexxh
-
map2k5
- medicine
Reaction
release of an N-terminal dipeptide from a peptide comprising four or additional information residues, with broad specificity. Also acts on dipeptidyl 2-naphthylamides. =
Synonyms
BT_1846, Cabys_2252, dipeptdiyl peptidase III, dipeptidyl aminopeptidase III, dipeptidyl arylamidase III, dipeptidyl peptidase III, dipeptidyl-peptidase III, dipeptidyl-peptide hydrolase, dipeptidylpeptidase III, DPP III, DPP-3, DPP-III, DPP3, DPPIII, enkephalinase B, NUDT3, peptidase, dipeptidyl, III, PG_0317, PHYPA_007037, red cell angiotensinase
ECTree
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Metals Ions
Metals Ions on EC 3.4.14.4 - dipeptidyl-peptidase III
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Co2+
Cu2+
Zinc
Zn2+
additional information
Co2+
516% activity in the presence of 0.1 mM Co2+, 758% activity in the presence of 1 mM Co2+
Cu2+
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activity of the cupric derivative for Lys-Ala-beta-naphthylamide is about 30% of that of the wild-type zinc enzyme. The enzyme activity of mutant Cu(II)-del-DPP III, in which Leu453 is deleted from the metal-binding motif, is only 1-2% of the enzyme activity of del-DPP III. The EPR spectra of Cu(II) del-DPP III do not change in the presence of excess Lys-Ala-beta-naphthylamide. The deletion of Leu453 from the HELLGH motif of rat DPP III leads to a complete loss of flexibility in the ligand geometry around the cupric ions
Zinc
the zinc ion is essential for the enzyme activity. It is positioned in the lower part of the upper domain where it is pentacoordinated by two histidines
Zn2+
QM/MM calculations reveal that the 5-coordinated metal ion is more favourable than the 6-coordinated one in only the most compact DPP III form. In this structure E451 is H-bonded to the metal ion coordinating water. Constraints for the broad substrate specificity of DPP III are the possibility of the substrate adopting the beta-strand shape and its charged N-terminus. The active conformation of the enzyme is the most compact form
additional information
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spectral analysis of Zn2+-, Ni2+-, Cu2+-, Co2+-substituted enzyme