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Ligand Arg-Pro-Lys-Pro-Gln-Gln Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Basic Ligand Information Molecular Structure
C3 2 H5 6 N1 2 O9
Arg-Pro-Lys-Pro-Gln-Gln
UFTDINHLCHPVEW-LLINQDLYSA-N
Roles as Enzyme Ligand
Product in Enzyme-catalyzed Reactions (5 results)
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RPKPQQFFGLM + H2O = RPKPQQ + L-Phe + FGLM
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Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2 + H2O = Arg-Pro-Lys-Pro-Gln-Gln + Phe-Phe-Gly-Leu-Met-NH2
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Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2 + H2O = Arg-Pro-Lys-Pro-Gln + Gln-Phe-Phe-Gly-Leu-Met-NH2 + Arg-Pro-Lys-Pro-Gln-Gln + Phe-Phe-Gly-Leu-Met-NH2 + Arg-Pro-Lys-Pro
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Substance P + H2O = Arg-Pro-Lys-Pro-Gln-Gln + Phe + Phe-Gly + Leu-Met-NH2
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Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2 + H2O = Arg-Pro-Lys-Pro-Gln-Gln + Phe-Phe-Gly + Leu-Met-NH2
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Enzyme Kinetic Parameters
References & Links Literature References (3)
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Purification and substrate specificity of a strongly hydrophobic extracellular metalloendopeptidase (gelatinase) from Streptococcus faecalis (strain 0G1-10)
1989
Mäkinen, P.L.; Clewell, D.B.; An, F.; Mäkinen, K.K.
J. Biol. Chem.
264
3325-3334
The specificity of sea urchin hatching enzyme (envelysin) places it in the mammalian matrix metalloproteinase family
1991
Nomura, K.; Tanaka, H.; Kikkawa, Y.; Yamaguchi, M.; Suzuki, N.
Biochemistry
30
6115-6123
Specificity of action on neuropeptides of an endopeptidase from the synaptosomal membranes of guinea pig brain
1988
Yoshikawa, S.; Tashiro, T.; Takahashi, K.
J. Biochem.
104
1007-1010
Links to other databases for Arg-Pro-Lys-Pro-Gln-Gln