‘Species’ of peptidases
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Alan J. Barrett
Abstract
A good system for the naming and classification of peptidases can contribute much to the study of these enzymes. Having already described the building of families and clans in the MEROPS system, we here focus on the lowest level in the hierarchy, in which the huge number of individual peptidase proteins are assigned to a lesser number of what we term ‘species’ of peptidases. Just over 2000 peptidase species are recognised today, but we estimate that 25 000 will one day be known. Each species is built around a peptidase protein that has been adequately characterised. The cluster of peptidase proteins that represent the single species is then assembled primarily by analysis of a sequence ‘tree’ for the family. Each peptidase species is given a systematic identifier and a summary page of data regarding it is assembled. Because the characterisation of new peptidases lags far behind the sequencing, the majority of peptidase proteins are so far known only as amino acid sequences and cannot yet be assigned to species. We suggest that new forms of analysis of the sequences of the unassigned peptidases may give early indications of how they will cluster into the new species of the future.
©2007 by Walter de Gruyter Berlin New York
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Artikel in diesem Heft
- Proteinase Inhibitors and Biological Control – An Attractive International Symposia Series
- Two decades of thyroglobulin type-1 domain research
- Cysteine cathepsin non-inhibitory binding partners: modulating intracellular trafficking and function
- Cysteine proteases: destruction ability versus immunomodulation capacity in immune cells
- ‘Species’ of peptidases
- Protease research in the era of systems biology
- Human and mouse homo-oligomeric meprin A metalloendopeptidase: substrate and inhibitor specificities
- Association of cathepsin E with tumor growth arrest through angiogenesis inhibition and enhanced immune responses
- Characterization and comparative 3D modeling of CmPI-II, a novel ‘non-classical’ Kazal-type inhibitor from the marine snail Cenchritis muricatus (Mollusca)
- Cellular localization of MAGI-1 caspase cleavage products and their role in apoptosis
- Differential methylation kinetics of individual target site strands by T4Dam DNA methyltransferase
- Characterisation of zinc-binding domains of peroxisomal RING finger proteins using size exclusion chromatography/inductively coupled plasma-mass spectrometry
- Defining the extended substrate specificity of kallikrein 1-related peptidases
- Latent MMP-9 is bound to TIMP-1 before secretion
- Novel expression of kallikreins, kallikrein-related peptidases and kinin receptors in human pleural mesothelioma
- Activity of ulilysin, an archaeal PAPP-A-related gelatinase and IGFBP protease
- Clinical chemistry reference database for Wistar rats and C57/BL6 mice
