The substrate range of tripeptidyl-peptidase I

European Journal of Paediatric Neurology

Volumn 5, Issue , 2001, Pages 69-72

  Bernardini, F ^a   Warburton, M J ^a  

^a ST GEORGE'S UNIVERSITY OF LONDON   (United Kingdom)

Author keywords

Late infantile neuronal ceroid lipofuscinosis; Peptide degradation; Tripeptidyl peptidase I

Indexed keywords

CLN 2 PROTEIN; EXOPEPTIDASE; GENE PRODUCT; PEPTIDE; TRIPEPTIDE; TRIPEPTIDYL PEPTIDASE I; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; ENZYME SPECIFICITY; ENZYME SUBSTRATE; GENE MUTATION; MOLECULAR SIZE; MOLECULAR WEIGHT; NEURONAL CEROID LIPOFUSCINOSIS; NONHUMAN; PHYSIOLOGY; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN STRUCTURE;

BINDING SITES; ENDOPEPTIDASES; HUMANS; INFANT; MOLECULAR WEIGHT; NEURONAL CEROID-LIPOFUSCINOSES; PEPTIDE FRAGMENTS; SUBSTRATE SPECIFICITY;

EID: 0034916404     PISSN: 10903798     EISSN: None     Source Type: Journal    
DOI: 10.1053/ejpn.2000.0438     Document Type: Article

References (10)

1. Classical late infantile neuronal ceroid lipofuscinosis fibroblasts are deficient in lysosomal tripeptidyl peptidase-I
2. Tripeptidyl peptidase-I deficiency in classical late infantile neuronal ceroid lipofuscinosis brain tissue. Evidence for defective peptidase rather than proteinase activity
3. Purification and characterisation of a tripeptidyl aminopeptidase-I from rat spleen
4. Association of mutations in a lysosomal protein with classical late infantile neuronal ceroid lipofuscinosis
5. Partial purification and characterisation of an ovarian tripeptidyl peptidase: A lysosomal exopeptidase that sequentially releases collagen-related (Gly-Pro-X) triplets
6. Purification and characterization of a tripeptidyl peptidase from human osteoclastomas: Evidence for its role in bone resorption
7. Characterization of endopeptidase activity of tripeptidyl peptidase-I/CLN2 protein which is deficient in classical late infantile neuronal ceroid lipofuscinosis
8. Specific storage of subunit c of mitochondrial ATP synthase in lysosomes of neuronal ceroid lipofuscinosis (Batten's disease)
9. Decreased lysosomal subunit c-degrading activity in fibroblasts from patients with late infantile neuronal ceroid lipofuscinosis
10. Prolyl oligopeptidase: An unusual β-propeller domain regulates proteolysis