3.4.13.18: cytosol nonspecific dipeptidase
This is an abbreviated version!
For detailed information about cytosol nonspecific dipeptidase, go to the full flat file.
Word Map on EC 3.4.13.18
Reaction
hydrolysis of dipeptides, preferentially hydrophobic dipeptides including prolyl amino acids
=
Synonyms
carboxypeptidase of glutamate like-B, CG17337, CNDP2, CPGL, CPGL-B, diglycinase, dipeptidase, glycylglycine, DPP8, DPP8-v3, EC 3.4.13.1, EC 3.4.13.11, EC 3.4.13.13, EC 3.4.13.15, EC 3.4.13.2, EC 3.4.13.3, EC 3.4.13.8, EC 3.4.3.1, EC 3.4.3.2, EC 3.4.3.3, EC 3.4.3.6, Gly-Leu hydrolase, glycyl-glycine dipeptidase, glycyl-L-leucine dipeptidase, glycyl-L-leucine hydrolase, glycyl-L-leucine peptidase, glycyl-leucine dipeptidase, glycylleucine dipeptidase, glycylleucine dipeptide hydrolase, glycylleucine hydrolase, glycylleucine peptidase, human cytosolic non-specific dipeptidase, iminodipeptidase, L-amino-acyl-L-amino-acid hydrolase, L-prolylglycine dipeptidase, N2-beta-alanylarginine dipeptidase, non-specific dipeptidase, PepD, Peptidase A, Pro-X dipeptidase, Pro-Xaa dipeptidase, prolinase, prolyl dipeptidase
ECTree
Metals Ions
Metals Ions on EC 3.4.13.18 - cytosol nonspecific dipeptidase
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Mg2+
-
favors the activity towards the substrates Leu-Gly and Ala-Gly
Ni2+
-
about 75% of the activation with Co2+
additional information
-
no activation by Cd2+, Zn2+
Co2+
-
when substrates are cleaved rapidly by dipeptidase, addition of Co2+ inhibits the reaction. The more slowly a substrate is hydrolyzed in the absence of metals, the greater the activating effect, activation is not accompanied by change in Km
Co2+
-
enzyme contains two binding sites
Co2+
-
hydrolysis of the relative poor substrates, Pro-Gly and Gly-Gly is activated, whereas that of Ala-Gly is inhibited
Co2+
-
inhibits Ala-Gly hydrolysis, activates Leu-Gly hydrolysis
Co2+
-
complex pattern of inhibition or activation with different dipeptide substrates
Mn2+
-
activates
Mn2+
-
when substrates are cleaved rapidly by dipeptidase, addition of Mn2+ inhibits the reaction. The more slowly a substrate is hydrolyzed in the absence of metals, the greater the activating effect, activation is accompanied by an increase in Km
Mn2+
-
two binding sites, at least one of which is distinct from a Co2+ site
Mn2+
-
0.1 mM, increases prolinase activity in normal erythrocytes against Pro-Gly, Pro-Glu, Pro-Leu, Pro-Ser and Pro-Phe
Mn2+
-
hydrolysis of the relative poor substrates, Pro-Gly and Gly-Gly is activated, whereas that of Ala-Gly is inhibited
Mn2+
-
favors the activity towards the substrates Leu-Gly and Ala-Gly
Mn2+
-
about 35% of the activation with Co2+
Mn2+
-
complex pattern of inhibition or activation with different dipeptide substrates
Zn2+
-
Zn2+ inhibits, but activates in phosphate buffer
Zn2+
-
possibly contains 1 mol of Zn2+ per mol of enzyme
Zn2+
-
0.9 gatom of zinc per mol of enzyme
Zn2+
-
0.1 mM Zn2+ activates