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
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Synonyms
Synonyms on EC 3.4.14.9 - tripeptidyl-peptidase I
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aminopeptidase, tripeptidyl, I
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AO090166000084
ceroid lipofuscinosis 2 protease
CLN2
EC 3.4.14.8
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formerly, part transferred
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LPIC
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lysosomal pepstatin insensitive protease
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SedD
TPP I
TPP-I
Tpp1
TPPI
tripeptidyl aminopeptidase
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tripeptidyl aminopeptidase I
tripeptidyl peptidase
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tripeptidyl peptidase 1
tripeptidyl peptidase I
tripeptidyl-peptidase 1
TTP-I
TPP I
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prefers Leu, Phe and Nle at the P1 position, whereas Asn, His, Lys, Arg, Ser, Val, Ile, Thr, Gly and Pro are highly unfavored in this position, showing less than 1% of the activity of the best substrates
Tpp1
TPP1 is a serine protease that possesses two catalytic functions, a primary tripeptidyl exopeptidase activity with a pH optimum of about 5.0 that catalyzes the sequential release of tripeptides from the unsubstituted N termini of substrates and a much weaker endoproteolytic activity with a pH optimum of about 3.0
tripeptidyl peptidase I
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shows tripeptidyl peptidase activity and pepstatin insensitive carboxyl endopeptidase activity