ArticleThe protein journal2008
Structural organization of precursors of thermolysin-like proteinases.
Article in The protein journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Protease S of entomopathogenic bacterium Photorhabdus laumondii: expression, purification and effect on greater wax moth Galleria mellonella.Molecular biology reports · 2024Article
- Assay for Protealysin-like Protease Inhibitor Activity.Bio-protocol · 2022Article
- Salt Mediated Modulation of Autolysis of Thermolysin-Like Proteinase, Salilysin, Isolated from a Moderate Halophile, Chromohalobacter salexigens DSM3043.The protein journal · 2021Article
- Bacterial Actin-Specific Endoproteases Grimelysin and Protealysin as Virulence Factors Contributing to the Invasive Activities ofInternational journal of molecular sciences · 2020Review
- An Internally Quenched Fluorescent Peptide Substrate for Protealysin.Scientific reports · 2019Article
- Bacillus licheniformis BlaR1 L3 loop is a zinc metalloprotease activated by self-proteolysis.PloS one · 2012Article
- Structural basis for the autoprocessing of zinc metalloproteases in the thermolysin family.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Proenzyme structure and activation of astacin metallopeptidase.The Journal of biological chemistry · 2010Article
- Crystal structure of the protealysin precursor: insights into propeptide function.The Journal of biological chemistry · 2010Article
- Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The primary structures of the full-length precursors of thermolysin-like proteinases (TLPs) were systemically analyzed. Structural comparison of the precursor amino-terminal regions (ATRs) removed during maturation allowed us to divide the family into two groups: peptidases with short (about 50 amino acids) and long (about 200 amino acids) ATRs. The accumulation of mutations in the ATRs of both types proved to correlate with that in the catalytic domains. No classical signal peptides were identified in the short ATRs, but they contained a conserved PPL-motif near the initiation methionine. The functional role of the short ATRs and PPL-motif is currently unclear. The C-terminal regions (CTRs) of TLP precursors, which are often removed during maturation, too, are found in about a half of precursors with long ATRs, but occur more rarely in precursors with short ATRs. CTRs in TLP precursors contain previously identified conserved domains typical for many other proteins and likely underlie the interaction with high molecular weight substrates.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.