Ser475, Glu272, Asp276, Asp327, and Asp360 are involved in catalytic activity of human tripeptidyl-peptidase I

FEBS Letters

Volumn 579, Issue 6, 2005, Pages 1383-1388

  Walus, Mariusz ^a   Kida, Elizabeth ^a   Wisniewski, Krystyna E ^a   Golabek, Adam A ^a  

^a NEW YORK STATE INSTITUTE FOR BASIC RESEARCH IN DEVELOPMENTAL DISABILITIES   (United States)

Author keywords

Active site; CLN2 protein; Mutagenesis; Sedolisin; Serine carboxyl peptidase; Tripeptidyl peptidase I

Indexed keywords

AMINOPEPTIDASE; ASPARTIC ACID; CARBOXYL GROUP; GLUTAMIC ACID; SERINE; TRIPEPTIDE DERIVATIVE; TRIPEPTIDYL PEPTIDASE I; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CATALYSIS; CHO CELL; HUMAN; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS;

MAMMALIA;

EID: 14244262812     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2005.01.035     Document Type: Article

References (29)

1. S. Murao, K. Oda, and Y. Matsushita New acid proteases from Scytalidium lignicolum M-133 Agric. Biol. Chem. 36 1972 1647 1650
2. K. Oda, M. Sugitani, K. Fukuhara, and S. Murao Purification and properties of a pepstatin-insensitive carboxyl proteinase from a gram-negative bacterium Biochim. Biophys. Acta 923 1987 463 469
3. S. Murao, K. Ohkuni, M. Nagao, K. Hirayama, K. Fukuhara, K. Oda, H. Oyama, and T. Shin Purification and characterization of kumamolysin, a novel thermostable pepstatin-insensitive carboxyl proteinase from Bacillus novosp. MN-32 J. Biol. Chem. 268 1993 349 355
4. H.S. Toogood, M. Prescott, and R.M. Daniel A pepstatin-insensitive aspartic proteinase from a thermophilic Bacillus sp Biochem. J. 307 1995 783 789
5. M. Shibata, B.M. Dunn, and K. Oda Substrate specificity of pepstatin-insensitive carboxyl proteinase from Bacillus coagulans J-4 J. Biochem. 124 1998 642 647
6. H.K. Kwon, H. Kim, and T.I. Ahn Pepstatin-insensitive carboxyl proteinase: a biochemical marker for late lysosomes in Amoeba proteus Korean J. Biol. Sci. 3 1999 221 228
7. A. Wlodawer, M. Li, A. Gustchina, H. Oyama, B.M. Dunn, and K. Oda Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases Acta Biochim. Pol. 50 2003 81 102
8. A. Wlodawer, M. Li, Z. Dauter, A. Gustchina, K. Uchida, H. Oyama, B.M. Dunn, and K. Oda Carboxyl proteinase from Pseudomonas defines a novel family of subtilisin-like enzymes Nat. Struct. Biol. 8 2001 442 446
9. M. Comellas-Bigler, P. Fuentes-Prior, K. Maskos, R. Huber, H. Oyama, K. Uchida, B.M. Dunn, K. Oda, and W. Bode The 1.4 Å crystal structure of kumamolysin: a thermostable serine carboxyl type proteinase Structure 10 2002 865 876
10. D.E. Sleat, R.J. Donnelly, H. Lackland, C.G. Liu, I. Sohar, R.K. Pullarkat, and P. Lobel Association of mutations in a lysosomal protein with classical late-infantile neuronal ceroid lipofuscinosis Science 277 1997 1802 1805
11. D.E. Sleat, R.M. Gin, I. Sohar, K.E. Wisniewski, S. Sklower Brooks, R. Pullarkat, D.N. Palmer, T.J. Lerner, R.M. Boustany, P. Uldall, A.N. Siakotos, R.J. Donnelly, and P. Lobel Am. J. Hum. Genet. 64 1999 1511 1523
12. A.E. Page, K. Fuller, T.J. Chambers, and M.J. Warburton Purification and characterization of a tripeptidyl peptidase I from human osteoclastomas: evidence for its role in bone resorption Arch. Biochem. Biophys. 307 1993 354 359
13. Y. Watanabe, Y. Kumagai, and Y. Fujimoto Acidic tripeptidyl aminopeptidase in rat liver tritosomes: partial purification and determination of its primary substrate specificity Biochem. Int. 27 1992 869 877
14. D. Vines, and M.J. Warburton Purification and characterisation of a tripeptidyl aminopeptidase I from rat spleen Biochim. Biophys. Acta 1384 1998 233 242
15. J. Ezaki, M. Takeda-Ezaki, K. Oda, and E. Kominami Characterization of endopeptidase activity of tripeptidyl peptidase-I/CLN2 protein which is deficient in classical late infantile neuronal ceroid lipofuscinosis Biochem. Biophys. Res. Commun. 268 2000 904 908
16. L. Lin, I. Sohar, H. Lackland, and P. Lobel The human CLN2 protein/tripeptidyl-peptidase I is a serine protease that autoactivates at acidic pH J. Biol. Chem. 276 2001 2249 2255
17. M.A. Junaid, G. Wu, and R.K. Pullarkat Purification and characterization of bovine brain lysosomal pepstatin-insensitive proteinase, the gene product deficient in the human late-infantile neuronal ceroid lipofuscinosis J. Neurochem. 74 2000 287 294
18. N.D. Rawlings, and A.J. Barrett Families of serine peptidases Meth. Enzymol. 244 1994 19 61
19. A.A. Golabek, E. Kida, M. Walus, P. Wujek, P. Mehta, and K.E. Wisniewski Biosynthesis, glycosylation, and enzymatic processing in vivo of human tripeptidyl-peptidase I J. Biol. Chem. 278 2003 7135 7145
20. P. Wujek, E. Kida, M. Walus, K.E. Wisniewski, and A.A. Golabek N-glycosylation is crucial for folding, trafficking, and stability of human tripeptidyl-peptidase I J. Biol. Chem. 279 2004 12827 12839
21. E. Kida, A.A. Golabek, M. Walus, P. Wujek, W. Kaczmarski, and K.E. Wisniewski Distribution of tripeptidyl peptidase I in human tissues under normal and pathological conditions J. Neuropathol. Exp. Neurol. 60 2001 280 292
22. S.N. Ho, H.D. Hunt, R.M. Horton, J.K. Pullen, and L.R. Pease Site-directed mutagenesis by overlap extension using the polymerase chain reaction Gene 77 1989 51 59
23. Golabek, A.A., Walus, M., Wisniewski, K.E. and Kida, E. (2004) Glycosaminoglycans modulate activation, activity, and stability of tripeptidyl-peptidase I in vitro and in vivo. J. Biol. Chem. Dec 6 [Epub ahead of print]
24. A. Wlodawer, S.R. Durell, M. Li, H. Oyama, K. Oda, and B.M. Dunn A model of tripeptidyl-peptidase I (CLN2), a ubiquitous and highly conserved member of the sedolisin family of serine-carboxyl peptidases BMC Struct. Biol. 3 2003 8
25. C.-G. Liu, D.E. Sleat, R.J. Donnelly, and P. Lobel Structural organization and sequence of CLN2, the defective gene in classical late infantile neuronal ceroid lipofuscinosis Genomics 50 1998 206 212
26. J. Ezaki, I. Tanida, N. Kanehagi, and E. Kominami A lysosomal proteinase, the late infantile neuronal ceroid lipofuscinosis gene (CLN2) product, is essential for degradation of a hydrophobic protein, the subunit c of ATP synthase J. Neurochem. 72 1999 2573 2582
27. B. Tsai, Y. Ye, and T.A. Rapoport Retro-translocation of proteins from the endoplasmic reticulum into the cytosol Nat. Rev. Mol. Cell Biol. 3 2002 246 255
28. A.A. Golabek, P. Wujek, M. Walus, S. Bieler, C. Soto, K.E. Wisniewski, and E. Kida Maturation of human tripeptidyl-peptidase I in vitro J. Biol. Chem. 279 2004 31058 31067
29. H. Oyama, S. Abe, S. Ushiyama, S. Takahashi, and K. Oda Identification of catalytic residues of pepstatin-insensitive carboxyl proteinases from prokaryotes by site-directed mutagenesis J. Biol. Chem. 274 1999 27815 27822