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Ligand Val-Val Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Basic Ligand Information Molecular Structure
C1 0 H2 0 N2 O3
Val-Val
KRNYOVHEKOBTEF-YUMQZZPRSA-N
L-Val-L-Val, L-Val-L-Val[side 2], L-valyl-L-valine, Val-Val-OH
Roles as Enzyme Ligand
Substrate in Enzyme-catalyzed Reactions (1 result)
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ATP + L-valine + L-Val-L-Val = ADP + phosphate + L-Val-L-Val-L-Val
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Product in Enzyme-catalyzed Reactions (4 results)
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GPGRVV + H2O = GPGR + Val-Val
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SPGRVV + H2O = SPGR + Val-Val
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ATP + 2 L-valine = ADP + phosphate + L-Val-L-Val
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ATP + H2O + L-Val-L-Val-[L-Val-L-Val-binding protein][side 1] = ADP + phosphate + L-Val-L-Val[side 2] + [L-Val-L-Val-binding protein][side 1]
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Inhibitor in Enzyme-catalyzed Reactions (2 results)
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Enzyme Kinetic Parameters
Ki Value (2 results)
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References & Links Literature References (4)
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Rat intestinal brush border membrane dipeptidyl-aminopeptidase IV: kinetic properties and substrate specificities of the purified enzyme
1982
Bella, A.M.; Erickson, R.H.; Kim, Y.S.
Arch. Biochem. Biophys.
218
156-162
Inhibitors of tripeptidyl peptidase II. 2. Generation of the first novel lead inhibitor of cholecystokinin-8-inactivating peptidase: a strategy for the design of peptidase inhibitors
2000
Ganellin, C.R.; Bishop, P.B.; Bambal, R.B.; Chan, S.M.; Law, J.K.; Marabout, B.; Luthra, P.M.; Moore, A.N.; Peschard, O.; Bourgeat, P.; Rose, C.; Vargas, F.; Schwartz, J.C.
J. Med. Chem.
43
664-674
Negative selectivity and the evolution of protease cascades: the specificity of plasmin for peptide and protein substrates
2000
Hervio, L.S.; Coombs, G.S.; Bergstrom, R.C.; Trivedi, K.; Corey, D.R.; Madison, E.L.
Chem. Biol.
7
443-453
New L-amino acid ligases catalyzing oligopeptide synthesis from various microorganisms
2010
Arai, T.; Kino, K.
Biosci. Biotechnol. Biochem.
74
1572-1577
Links to other databases for Val-Val
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