Folding incompetence of cathepsin L-like cysteine proteases may be compensated by the highly conserved, domain-building N-terminal extension of the proregion

Biological Chemistry

Volumn 382, Issue 5, 2001, Pages 859-865

  Schilling, K ^a   Pietschmann, S ^a   Fehn, M ^a   Wenz, I ^a   Wiederanders, B ^a  

^a JENA UNIVERSITY HOSPITAL   (Germany)

Author keywords

Cathepsin S; Foldase; Inhibition kinetics; Papain family; Propeptide; Scanning mutagenesis

Indexed keywords

AMINO ACID; CATHEPSIN L; CATHEPSIN S; CYSTEINE PROTEINASE; PAPAIN;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME STRUCTURE; HYPOTHESIS; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN FOLDING;

CATHEPSINS; CONSERVED SEQUENCE; CYSTEINE ENDOPEPTIDASES; ENZYME PRECURSORS; HUMANS; KINETICS; MODELS, CHEMICAL; MUTAGENESIS; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY;

EID: 0034941496     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.2001.105     Document Type: Article

References (31)

1. Possible role for water dissociation in the slow binding of phosphorus-containing transition-state-analogue inhibitors of thermolysin
2. The slow-binding inhibition of cathepsin K by its propeptide
3. Investigation of diffusion-limited rates of chymotrypsin reactions by viscosity variation
4. Catalysis of a protein folding reaction: Mechanistic implications of the 2.0 A structure of the subtilisin-prodomain complex
5. Trifluoroethanol and colleagues: Cosolvents come of age. Recent studies with peptides and proteins
6. Potency and selectivity of the cathepsin L propeptide as an inhibitor of cysteine proteases
7. Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment
8. Proregion structure of members of the papain superfamily. Mode of inhibition of enzymatic activity
9. Potent slow-binding inhibition of cathepsin B by its propeptide
10. Potency and selectivity of inhibition of cathepsin K, L and S by their respective propeptides
11. pH-induced conformational transitions of the propeptide of human cathepsin L. A role for a molten globule state in zymogen activation
12. Two distinct gene subfamilies within the family of cysteine protease genes
13. An evolutionarily conserved tripartite tryptophan motif stabilizes the prodomains of cathepsin L-like cysteine proteases
14. Inhibition of trypanosomal cysteine proteinases by their propeptides
15. The crystal structure of human procathepsin K
16. The inhibition of cathepsin S by its propeptide-specificity and mechanism of action
17. Crystal structure of human cathepsin S
18. In vivo expression of an alternatively spliced human tumor message that encodes a truncated form of cathepsin B. Subcellular distribution of the truncated enzyme in COS cells
19. The behaviour and significance of slow-binding enzyme inhibitors
20. Human cathepsin X: A novel cysteine protease of the papain family with a very short proregion and unique insertions
21. Inhibition of carcinoma cell invasion and liver metastases formation by the cysteine proteinase inhibitor E-64
22. Two-step mechanism of inhibition of cathepsin B by cystatin C due to displacement of the proteinase occluding loop
23. Function of the propeptide region in recombinant expression of active procathepsin L in Escherichia coli
24. Crystal structure of wild-type human procathepsin K
25. Crystal structure of human procathepsin X: A cysteine protease with the proregion covalently linked to the active site cysteine
26. Activity and deletion analysis of recombinant human cathepsin L expressed in Escherichia coli
27. Unfolded conformations of alpha-lytic protease are more stable than its native state
28. The proregion of cathepsin L is required for proper folding, stability, and ER exit
29. The function of propeptide domains of cysteine proteinases
30. Proregion of Bombyx mori cysteine proteinase functions as an intramolecular chaperone to promote proper folding of the mature enzyme