3.4.21.100: sedolisin
This is an abbreviated version!
For detailed information about sedolisin, go to the full flat file.
Word Map on EC 3.4.21.100
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3.4.21.100
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peptidase
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proteinases
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subtilisins
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merops
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ceroid
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pcp
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lipofuscinosis
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tripeptidyl-peptidase
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diazoacetyl-dl-norleucine
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subtilisin-like
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prosegment
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tripeptidyl
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b-chain
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1,2-epoxy-3-p-nitrophenoxypropane
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coagulans
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medicine
- 3.4.21.100
- peptidase
- proteinases
- subtilisins
- merops
-
ceroid
- pcp
- lipofuscinosis
-
tripeptidyl-peptidase
- diazoacetyl-dl-norleucine
-
subtilisin-like
- prosegment
-
tripeptidyl
- b-chain
-
1,2-epoxy-3-p-nitrophenoxypropane
-
coagulans
- medicine
Reaction
Hydrolysis of the B chain of insulin at -Glu13-/-Ala-, -Leu15-/-Tyr- and -Phe25-/-Tyr-, and angiotensin I at -Tyr4-/-Ile-. A good synthetic substrate is Lys-Pro-Ile-Glu-Phe-/-Phe(NO2)-Arg-Leu =
Synonyms
EC 3.4.23.37, grifolisin, PCP, Pepstatin-insensitive carboxyl proteinase, PSCP, pseudomonalisin, pseudomonapepsin, Pseudomonas serine-carboxyl proteinase, Pseudomonas sp. pepstatin-insensitive carboxyl proteinase, scytalidolisin, scytalidopepsin A, SedA, SedB, SedC, SedD, sedolisin
ECTree
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Inhibitors
Inhibitors on EC 3.4.21.100 - sedolisin
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1,2-epoxy-3-(4-nitrophenoxy)propane
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modifies the enzyme with concomitant loss of activity
N,N'-dicyclohexylcarbodiimide
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inhibitor binds to Asp140 and Glu222 of the enzyme, inactivation with pseudo-first-order kinetics, inactivation is prevented by a competitive inhibitor, tyrostatin
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two molecules of the inhibitor are bound in the active site of the enzyme
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not inhibitory: pepstatin, 1,10-phenanthroline, EDTA, N-ethylmaleimide
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additional information
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diazoacetyl-DL-norleucine methyl ester; diisopropyl fluorophosphate (1 mM); EDTA (1 mM); iodoacetic acid (1 mM); not: pepstatin; p-chloromercuribenzenesulfonic acid; phenyl methane sulfonyl fluoride (1 mM); Streptomyces pepsin inhibitor
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additional information
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insensitive to pepstatin, diazoacetyl-DL-norleucine methyl ester and 1,2-epoxy-3(p-nitrophenoxy)propane
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additional information
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not inhibited by pepstatin. The hydrophilic nature of the S2' subsite appears to be a distinguishing feature of pepstatin-insensitive carboxyl proteinases
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