Nucleic Acids Research Advance Access originally published online on November 8, 2007
Nucleic Acids Research 2008 36(Database issue):D320-D325; doi:10.1093/nar/gkm954
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Nucleic Acids Research, 2008, Vol. 36, Database issue D320-D325
© 2007 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
This article appears in the following Nucleic Acids Research issue: Database issue [View the issue table of contents]
Articles |
MEROPS: the peptidase database
The Wellcome Trust Sanger Institute, Wellcome Trust Genome Campus, Hinxton, Cambridgeshire, CB10 1SA, UK
*To whom correspondence should be addressed. Tel: +44 1223 494983; Fax: +44 1223 494919; Email: ndr{at}sanger.ac.uk
Received September 17, 2007. Revised October 15, 2007. Accepted October 15, 2007.
Peptidases (proteolytic enzymes or proteases), their substrates and inhibitors are of great relevance to biology, medicine and biotechnology. The MEROPS database (http://merops.sanger.ac.uk) aims to fulfil the need for an integrated source of information about these. The organizational principle of the database is a hierarchical classification in which homologous sets of peptidases and protein inhibitors are grouped into protein species, which are grouped into families and in turn grouped into clans. Important additions to the database include newly written, concise text annotations for peptidase clans and the small molecule inhibitors that are outside the scope of the standard classification; displays to show peptidase specificity compiled from our collection of known substrate cleavages; tables of peptidase–inhibitor interactions; and dynamically generated alignments of representatives of each protein species at the family level. New ways to compare peptidase and inhibitor complements between any two organisms whose genomes have been completely sequenced, or between different strains or subspecies of the same organism, have been devised.
![]()
CiteULike
Connotea
Del.icio.us What's this?
This article has been cited by other articles:
![]() |
G. Debret, A. Martel, and P. Cuniasse RASMOT-3D PRO: a 3D motif search webserver Nucleic Acids Res., July 1, 2009; 37(suppl_2): W459 - W464. [Abstract] [Full Text] [PDF] |
||||
![]() |
D Bernardo, J A Garrote, I Nadal, A J Leon, C Calvo, L Fernandez-Salazar, A Blanco-Quiros, Y Sanz, and E Arranz Is it true that coeliacs do not digest gliadin? Degradation pattern of gliadin in coeliac disease small intestinal mucosa Gut, June 1, 2009; 58(6): 886 - 887. [Full Text] [PDF] |
||||
![]() |
A. Cedzich, F. Huttenlocher, B. M. Kuhn, J. Pfannstiel, L. Gabler, A. Stintzi, and A. Schaller The Protease-associated Domain and C-terminal Extension Are Required for Zymogen Processing, Sorting within the Secretory Pathway, and Activity of Tomato Subtilase 3 (SlSBT3) J. Biol. Chem., May 22, 2009; 284(21): 14068 - 14078. [Abstract] [Full Text] [PDF] |
||||
![]() |
C.-C. Wang, H.-C. Houng, C.-L. Chen, P.-J. Wang, C.-F. Kuo, Y.-S. Lin, J.-J. Wu, M. T. Lin, C.-C. Liu, W. Huang, et al. Solution Structure and Backbone Dynamics of Streptopain: INSIGHT INTO DIVERSE SUBSTRATE SPECIFICITY J. Biol. Chem., April 17, 2009; 284(16): 10957 - 10967. [Abstract] [Full Text] [PDF] |
||||
![]() |
A. H. Camp and R. Losick A feeding tube model for activation of a cell-specific transcription factor during sporulation in Bacillus subtilis Genes & Dev., April 15, 2009; 23(8): 1014 - 1024. [Abstract] [Full Text] [PDF] |
||||
![]() |
D. Baniulis, E. Yamashita, J. P. Whitelegge, A. I. Zatsman, M. P. Hendrich, S. S. Hasan, C. M. Ryan, and W. A. Cramer Structure-Function, Stability, and Chemical Modification of the Cyanobacterial Cytochrome b6f Complex from Nostoc sp. PCC 7120 J. Biol. Chem., April 10, 2009; 284(15): 9861 - 9869. [Abstract] [Full Text] [PDF] |
||||
![]() |
B.-B. Xie, F. Bian, X.-L. Chen, H.-L. He, J. Guo, X. Gao, Y.-X. Zeng, B. Chen, B.-C. Zhou, and Y.-Z. Zhang Cold Adaptation of Zinc Metalloproteases in the Thermolysin Family from Deep Sea and Arctic Sea Ice Bacteria Revealed by Catalytic and Structural Properties and Molecular Dynamics: NEW INSIGHTS INTO RELATIONSHIP BETWEEN CONFORMATIONAL FLEXIBILITY AND HYDROGEN BONDING J. Biol. Chem., April 3, 2009; 284(14): 9257 - 9269. [Abstract] [Full Text] [PDF] |
||||
![]() |
J. Haiko, M. Suomalainen, T. Ojala, K. Lahteenmaki, and T. K. Korhonen Invited review: Breaking barriers -- attack on innate immune defences by omptin surface proteases of enterobacterial pathogens Innate Immunity, April 1, 2009; 15(2): 67 - 80. [Abstract] [PDF] |
||||
![]() |
V. Quesada, G. R. Ordonez, L. M. Sanchez, X. S. Puente, and C. Lopez-Otin The Degradome database: mammalian proteases and diseases of proteolysis Nucleic Acids Res., January 1, 2009; 37(suppl_1): D239 - D243. [Abstract] [Full Text] [PDF] |
||||
![]() |
N. Padmanabhan, L. Fichtner, A. Dickmanns, R. Ficner, J. B. Schulz, and G. H. Braus The Yeast HtrA Orthologue Ynm3 Is a Protease with Chaperone Activity that Aids Survival Under Heat Stress Mol. Biol. Cell, January 1, 2009; 20(1): 68 - 77. [Abstract] [Full Text] [PDF] |
||||
![]() |
C.-T. Chen, E.-W. Yang, H.-J. Hsu, Y.-K. Sun, W.-L. Hsu, and A.-S. Yang Protease substrate site predictors derived from machine learning on multilevel substrate phage display data Bioinformatics, December 1, 2008; 24(23): 2691 - 2697. [Abstract] [Full Text] [PDF] |
||||
![]() |
M. J. Page and E. Di Cera Evolution of Peptidase Diversity J. Biol. Chem., October 31, 2008; 283(44): 30010 - 30014. [Abstract] [Full Text] [PDF] |
||||
![]() |
K. Kondas, G. Szlama, M. Trexler, and L. Patthy Both WFIKKN1 and WFIKKN2 Have High Affinity for Growth and Differentiation Factors 8 and 11 J. Biol. Chem., August 29, 2008; 283(35): 23677 - 23684. [Abstract] [Full Text] [PDF] |
||||
![]() |
P. K. Baral, N. Jajcanin-Jozic, S. Deller, P. Macheroux, M. Abramic, and K. Gruber The First Structure of Dipeptidyl-peptidase III Provides Insight into the Catalytic Mechanism and Mode of Substrate Binding J. Biol. Chem., August 8, 2008; 283(32): 22316 - 22324. [Abstract] [Full Text] [PDF] |
||||
![]() |
R. Bhaskaran, M. O. Palmier, J. L. Lauer-Fields, G. B. Fields, and S. R. Van Doren MMP-12 Catalytic Domain Recognizes Triple Helical Peptide Models of Collagen V with Exosites and High Activity J. Biol. Chem., August 1, 2008; 283(31): 21779 - 21788. [Abstract] [Full Text] [PDF] |
||||






