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Information on EC 3.4.22.B49 - cathepsin L1

for references in articles please use BRENDA:EC3.4.22.B49
preliminary BRENDA-supplied EC number
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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.B49 cathepsin L1
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This record set is specific for:
UNIPROT: Q7JNQ9
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Word Map
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The enzyme appears in viruses and cellular organisms
Reaction Schemes
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clear preference for Arg at P1 position (Lys, Glu, Thr, and Met are less efficient). FheCL1 shows distinct preference for hydrophobic amino acids in the P2, Leu is favored. Cathepsin L1 can accommodate Pro in the P2 position, but less efficiently than cathepsin L2. FheCL1 produces clear degradation fragments from collagen
Synonyms
cathepsin l1, ctsl1, fhcl1, fhecl1, catl1, fgcatl1h, cgctsl1, cpfhw, cathepsin l1h, da-ctsl1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cathepsin L1
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-
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cathepsin L1 proteinase
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-
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CL1
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-
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FheCL1
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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-
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CAS REGISTRY NUMBER
COMMENTARY hide
60616-82-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Leu-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
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-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
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-
-
?
benzyloxycarbonyl-Pro-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Pro-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
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-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0036 - 0.0044
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin
0.003 - 0.0242
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
0.1819 - 0.1912
benzyloxycarbonyl-Pro-Arg-7-amido-4-methylcoumarin
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
11 - 36.5
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin
2 - 24.7
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
1 - 1.7
benzyloxycarbonyl-Pro-Arg-7-amido-4-methylcoumarin
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q7JNQ9_FASHE
326
0
36773
TrEMBL
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Robinson, M.W.; Tort, J.F.; Lowther, J.; Donnelly, S.M.; Wong, E.; Xu, W.; Stack, C.M.; Padula, M.; Herbert, B.; Dalton, J.P.
Proteomics and phylogenetic analysis of the cathepsin L protease family of the helminth pathogen Fasciola hepatica: expansion of a repertoire of virulence-associated factors
Mol. Cell. Proteomics
7
1111-1123
2008
Fasciola hepatica (Q7JNQ9)
Manually annotated by BRENDA team