Purification and Characterization of Two Highly Thermophilic Alkaline Lipases from Thermosyntropha lipolytica
- Moh’d A. Salameh, J. Wiegel
- BiologyApplied and Environmental Microbiology
- 12 October 2007
ABSTRACT Two thermostable lipases were isolated and characterized from Thermosyntropha lipolytica DSM 11003, an anaerobic, thermophilic, alkali-tolerant bacterium which grows syntrophically with…
PRSS3/Mesotrypsin Is a Therapeutic Target for Metastatic Prostate Cancer
- Alexandra Hockla, E. Miller, Moh’d A. Salameh, J. Copland, D. Radisky, E. Radisky
- Biology, MedicineMolecular Cancer Research
- 1 December 2012
This study defines mesotrypsin as an important mediator of prostate cancer progression and metastasis, and suggests that inhibition of mesotypsin activity may provide a novel modality for prostate cancer treatment.
Lipases from extremophiles and potential for industrial applications.
- Moh’d A. Salameh, J. Wiegel
- BiologyAdvances in Applied Microbiology
- 2007
Biochemical and structural insights into mesotrypsin: an unusual human trypsin.
- Moh’d A. Salameh, E. Radisky
- BiologyInternational Journal of Biochemistry and…
- 13 September 2013
This review will explore the biochemical characteristics of mesotrypsin and structural insights into its specificity, function, and inhibition and suggest novel substrate specificity that hints at distinct physiological functions.
Effects of Detergents on Activity, Thermostability and Aggregation of Two Alkalithermophilic Lipases from Thermosyntropha lipolytica
- Moh’d A. Salameh, J. Wiegel
- BiologyOpen Biochemistry Journal
- 5 March 2010
Inhibitory assays of lipases using diisopropyl p-nitrophenylphosphate (E600) with increasing concentration of SDS and Tween 20 strongly suggest that SDS/Tween 20 do bind to the lid domain and/or active site pocket, thus promoting conformational changes that facilitate active site accessibility for the substrate.
Determinants of Affinity and Proteolytic Stability in Interactions of Kunitz Family Protease Inhibitors with Mesotrypsin*
- Moh’d A. Salameh, A. Soares, D. Navaneetham, D. Sinha, P. Walsh, E. Radisky
- BiologyJournal of Biological Chemistry
- 22 September 2010
The data suggest that the enhanced vulnerability of APPI to mesotrypsin cleavage may derive from sequence differences in the scaffold that propagate increased flexibility and mobility to the binding loop.
The P(2)' residue is a key determinant of mesotrypsin specificity: engineering a high-affinity inhibitor with anticancer activity.
- Moh’d A. Salameh, A. Soares, Alexandra Hockla, D. Radisky, E. Radisky
- Biology, ChemistryBiochemical Journal
- 15 November 2011
The results of the present study support the feasibility of engineering protein protease inhibitors of mesotrypsin and highlight their therapeutic potential.
Structural Basis for Accelerated Cleavage of Bovine Pancreatic Trypsin Inhibitor (BPTI) by Human Mesotrypsin*
- Moh’d A. Salameh, A. Soares, Alexandra Hockla, E. Radisky
- Biology, ChemistryJournal of Biological Chemistry
- 15 February 2008
Human mesotrypsin is an isoform of trypsin that displays unusual resistance to polypeptide trypsin inhibitors and has been observed to cleave several such inhibitors as substrates. Whereas…
The Amyloid Precursor Protein/Protease Nexin 2 Kunitz Inhibitor Domain Is a Highly Specific Substrate of Mesotrypsin*
- Moh’d A. Salameh, Jessica Robinson, E. Radisky
- Biology, ChemistryJournal of Biological Chemistry
- 17 November 2009
It is found that APP/protease nexin 2 is selectively cleaved by mesotrypsin within the Kunitz protease inhibitor domain, and cleavage of APPI compromises its inhibition of other serine proteases, including cationic trypsin and factor XIa, by 2 orders of magnitude.
Presence versus absence of hydrogen bond donor Tyr‐39 influences interactions of cationic trypsin and mesotrypsin with protein protease inhibitors
- Moh’d A. Salameh, Alexei S Soares, Alexandre P. Alloy, E. Radisky
- Biology, ChemistryProtein Science
- 1 August 2012
The results indicate that the presence of Ser‐39 in mesotrypsin, and corresponding absence of a single H‐bond to the inhibitor backbone, makes a small but significant functional contribution to the resistance of mesotRYpsin to inhibition and the ability of mesosynthesis to proteolyze inhibitors.
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