3.4.14.9: tripeptidyl-peptidase I
This is an abbreviated version!
For detailed information about tripeptidyl-peptidase I, go to the full flat file.
Word Map on EC 3.4.14.9
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3.4.14.9
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infantile
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neurodegenerative
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lincl
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late-infantile
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lipofuscinoses
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batten
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curvilinear
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palmitoyl-protein
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pepstatin-insensitive
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cdc28p
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serine-carboxyl
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lipopigments
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molecular biology
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diagnostics
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medicine
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analysis
- 3.4.14.9
-
infantile
- neurodegenerative
-
lincl
-
late-infantile
- lipofuscinoses
- batten
-
curvilinear
- palmitoyl-protein
-
pepstatin-insensitive
- cdc28p
-
serine-carboxyl
-
lipopigments
- molecular biology
- diagnostics
- medicine
- analysis
Reaction
Release of an N-terminal tripeptide from a polypeptide, but also has endopeptidase activity =
Synonyms
aminopeptidase, tripeptidyl, I, AO090166000084, ceroid lipofuscinosis 2 protease, CLN2, CLN2 protein, CLN2p, EC 3.4.14.8, LPIC, lysosomal pepstatin insensitive protease, N-terminal tripeptidyl exopeptidase, SedB, SedC, SedD, sedolisin B, sedolisin C, sedolisin D, TPP I, TPP-I, Tpp1, TPP1F, TPPI, tripeptidyl aminopeptidase, tripeptidyl aminopeptidase I, tripeptidyl exopeptidase, tripeptidyl peptidase, tripeptidyl peptidase 1, tripeptidyl peptidase I, tripeptidyl peptidase-I, tripeptidyl-peptidase 1, tripeptidyl-peptidase I, TTP-I, v4-7
ECTree
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Subunits
Subunits on EC 3.4.14.9 - tripeptidyl-peptidase I
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additional information
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x * 89000, fusion protein with enhanced green fluorescent protein, SDS-PAGE
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x * 89000, fusion protein with enhanced green fluorescent protein, SDS-PAGE
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x * 65000, TPPIF, SDS-PAGE, x * 75780, sequence calculation, x * 105000, recombinant GFP-tagged TPPIF, SDS-PAGE
the enzyme has a prodomain (residues 25-182) and a catalytic domain (peptidases S53 domain), which extends from residue 197 to the end. In TPP1F, the catalytic domain is interrupted by a stretch of amino acids (residues 370-499). The catalytic triad, a particular sequence of amino acids (S611, E272, D369 in TPP1F), which represent the catalytic residues and are highly conserved in the S53 sedolisin family of peptidases, to which TPP1 proteins belong, and a Ca2+ binding site are also present
additional information
-
the enzyme has a prodomain (residues 25-182) and a catalytic domain (peptidases S53 domain), which extends from residue 197 to the end. In TPP1F, the catalytic domain is interrupted by a stretch of amino acids (residues 370-499). The catalytic triad, a particular sequence of amino acids (S611, E272, D369 in TPP1F), which represent the catalytic residues and are highly conserved in the S53 sedolisin family of peptidases, to which TPP1 proteins belong, and a Ca2+ binding site are also present