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Ligand Leu-Gly-Pro Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Basic Ligand Information Molecular Structure
C1 3 H2 3 N3 O4
Leu-Gly-Pro
YFBBUHJJUXXZOF-UHFFFAOYSA-N
Roles as Enzyme Ligand
Substrate in Enzyme-catalyzed Reactions (1 result)
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Product in Enzyme-catalyzed Reactions (3 results)
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benzyloxycarbonyl-Gly-Pro-Leu-Gly-Pro + H2O = Leu-Gly-Pro + ?
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Benzyloxycarbonyl-Gly-Pro-Leu-Gly-Pro + H2O = Benzyloxycarbonyl-Gly-Pro + Leu-Gly-Pro
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Benzyloxycarbonyl-Gly-Pro-Leu-Gly-Pro + H2O = Benzyloxycarbonyl-Gly-Pro + Leu-Gly-Pro
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Inhibitor in Enzyme-catalyzed Reactions (1 result)
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Enzyme Kinetic Parameters
kcat Value (Turnover Number) (1 result)
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KM Value (1 result)
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IC50 Value (1 result)
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References & Links Literature References (5)
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Purification and characterization of a proteinase in the venom of Trimeresurus flavoviridis. Complete separation of the enzyme from hemorrhagic activity
1970
Takahashi, T.; Ohsaka, A.
Biochim. Biophys. Acta
198
293-307
Dipeptidyl peptidase IV, a kidney brush-border serine peptidase
1976
Kenny, A.J.; Booth, A.G.; George, S.G.; Ingram, J.; Kershaw, D.; Wood, E.J.; Young, A.R.
Biochem. J.
155
169-182
Structure and activity of angiotensin I converting enzyme inhibitory peptides derived from Alaskan pollack skin
2002
Byun, H.G.; Kim, S.K.
J. Biochem. Mol. Biol.
35
239-243
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Proline-specific endopeptidases
2003
Besedin, D.V.; Rudenskaya, G.N.
Russ. J. Bioorg. Chem.
29
1-17
Engagement of the S1, S1' and S2' subsites drives efficient catalysis of peptide bond hydrolysis by the M1-family aminopeptidase from Plasmodium falciparum
2012
Dalal, S.; Ragheb, D.R.; Klemba, M.
Mol. Biochem. Parasitol.
183
70-77
Links to other databases for Leu-Gly-Pro
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