The substrate range of tripeptidyl-peptidase I

Tripeptidyl-peptidase I (TPP-I) is an exopeptidase which removes tripeptides from the N-terminus of peptides.Mutations in TPP-I are responsible for late infantile neuronal ceroid lipofuscinosis (CLN2). The nature of the physiological substrates and the range and specificity of the enzyme are unclear...

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Bibliographic Details
Published in:European journal of paediatric neurology 2001, Vol.5, p.69-72
Main Authors: Bernardini, Francesca, Warburton, Michael J.
Format: Article
Language:English
Subjects:
Aminopeptidases
Binding Sites
Dipeptidyl-Peptidases and Tripeptidyl-Peptidases
Endopeptidases - chemistry
Endopeptidases - metabolism
Humans
Infant
Late infantile neuronal ceroid lipofuscinosis
Molecular Weight
Neuronal Ceroid-Lipofuscinoses - enzymology
Peptide degradation
Peptide Fragments - chemistry
Peptide Fragments - metabolism
Serine Proteases
Substrate Specificity
Tripeptidyl-peptidase I
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Description
Summary:Tripeptidyl-peptidase I (TPP-I) is an exopeptidase which removes tripeptides from the N-terminus of peptides.Mutations in TPP-I are responsible for late infantile neuronal ceroid lipofuscinosis (CLN2). The nature of the physiological substrates and the range and specificity of the enzyme are unclear. Previous experiments suggest that the enzyme can degrade small peptides but not proteins. Digestion of a range of peptides of different size by TTP-I suggests that the enzyme will degrade small peptides with an extended N-terminal domain but not structured peptides. In general, this cut-off occurs between masses of 4.5 kDa and 6 kDa. Reference to the structures of other peptidases suggests a mechanism for this size selectivity.
ISSN:1090-3798
1532-2130
DOI:10.1053/ejpn.2000.0438