Quantitative Correlation of Conformational Binding Enthalpy with Substrate Specificity of Serine Proteases
نویسندگان
چکیده
منابع مشابه
Quantitative Correlation of Conformational Binding Enthalpy with Substrate Specificity of Serine Proteases
Members of the same protease family show different substrate specificity, even if they share identical folds, depending on the physiological processes they are part of. Here, we investigate the key factors for subpocket and global specificity of factor Xa, elastase, and granzyme B which despite all being serine proteases and sharing the chymotrypsin-fold show distinct substrate specificity prof...
متن کاملHigh throughput substrate specificity profiling of serine and cysteine proteases using solution-phase fluorogenic peptide microarrays.
Proteases regulate numerous biological processes with a degree of specificity often dictated by the amino acid sequence of the substrate cleavage site. To map protease/substrate interactions, a 722-member library of fluorogenic protease substrates of the general format Ac-Ala-X-X-(Arg/Lys)-coumarin was synthesized (X=all natural amino acids except cysteine) and microarrayed with fluorescent cal...
متن کاملComparative Studies on Retroviral Proteases: Substrate Specificity
Exogenous retroviruses are subclassified into seven genera and include viruses that cause diseases in humans. The viral Gag and Gag-Pro-Pol polyproteins are processed by the retroviral protease in the last stage of replication and inhibitors of the HIV-1 protease are widely used in AIDS therapy. Resistant mutations occur in response to the drug therapy introducing residues that are frequently f...
متن کاملSubstrate recognition drives the evolution of serine proteases.
A method is introduced to identify amino acid residues that dictate the functional diversity acquired during evolution in a protein family. Using over 80 enzymes of the chymotrypsin family, we demonstrate that the general organization of the phylogenetic tree and its functional branch points are fully accounted for by a limited number of residues that cluster around the active site of the prote...
متن کاملComparison of the substrate specificity of two potyvirus proteases.
The substrate specificity of the nuclear inclusion protein a (NIa) proteolytic enzymes from two potyviruses, the tobacco etch virus (TEV) and tobacco vein mottling virus (TVMV), was compared using oligopeptide substrates. Mutations were introduced into TEV protease in an effort to identify key determinants of substrate specificity. The specificity of the mutant enzymes was assessed by using pep...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: The Journal of Physical Chemistry B
سال: 2016
ISSN: 1520-6106,1520-5207
DOI: 10.1021/acs.jpcb.5b10637