About: Study on Substrate Specificity at Subsites for Severe Acute Respiratory Syndrome Coronavirus 3CL Protease

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About: Study on Substrate Specificity at Subsites for Severe Acute Respiratory Syndrome Coronavirus 3CL Protease Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Study on Substrate Specificity at Subsites for Severe Acute Respiratory Syndrome Coronavirus 3CL Protease
Creator	Shan, Yu-Fei Xu, Gen-Jun
Source	Medline; PMC
abstract	Autocleavage assay and peptide-based cleavage assay were used to study the substrate specificity of 3CL protease from the severe acute respiratory syndrome coronavirus. It was found that the recognition between the enzyme and its substrates involved many positions in the substrate, at least including residues from P4 to P2′. The deletion of either P4 or P2′ residue in the substrate would decrease its cleavage efficiency dramatically. In contrast to the previous suggestion that only small residues in substrate could be accommodated to the S1′ subsite, we have found that bulky residues such as Tyr and Trp were also acceptable. In addition, based on both peptide-based assay and autocleavage assay, Ile at the P1′ position could not be hydrolyzed, but the mutant L27A could hydrolyze the Ile peptide fragment. It suggested that there was a stereo hindrance between the S1′ subsite and the side chain of Ile in the substrate. All 20 amino acids except Pro could be the residue at the P2′ position in the substrate, but the cleavage efficiencies were clearly different. The specificity information of the enzyme is helpful for potent anti-virus inhibitor design and useful for other coronavirus studies.
has issue date	2005-12-01(xsd:dateTime)
bibo:doi	10.1111/j.1745-7270.2005.00114.x
bibo:pmid	16331324
has license	no-cc
sha1sum (hex)	d9542d53e742a06e46d73452e96d0b0d6d758d3d
schema:url	https://doi.org/10.1111/j.1745-7270.2005.00114.x
resource representing a document's title	Study on Substrate Specificity at Subsites for Severe Acute Respiratory Syndrome Coronavirus 3CL Protease
has PubMed Central identifier	PMC7109883
has PubMed identifier	16331324
schema:publication	Acta Biochim Biophys Sin (Shanghai)
resource representing a document's body	covid:d9542d53e742a06e46d73452e96d0b0d6d758d3d#body_text
is schema:about of	named entity 'fragment' named entity 'studies' named entity 'Tyr' named entity 'residues' named entity 'residue' named entity 'All' named entity 'substrate' covid:arg/d9542d53e742a06e46d73452e96d0b0d6d758d3d named entity 'inhibitor' named entity 'enzyme' named entity 'deletion' named entity 'residue' named entity 'peptide' named entity 'cleavage' named entity 'substrate' named entity 'assay' named entity 'efficiency' named entity 'position' named entity '20 amino acids' named entity 'enzyme' named entity 'peptide fragment' named entity 'substrate specificity' named entity 'substrate' named entity 'substrate' named entity 'peptide-based' named entity 'hydrolyze' named entity 'Subsites' named entity 'substrate' named entity '1, 2' named entity 'lane 8' named entity 'Trp' named entity 'proenzyme' named entity 'SARS-CoV' named entity 'Gly' named entity 'DTT' named entity 'genome' named entity 'RP-HPLC' named entity 'active site' named entity 'protease' named entity 'protease' named entity 'SDS-PAGE' named entity 'N 31' named entity 'SARS-CoV' named entity 'Gly' named entity '3, 4' named entity 'Trp' named entity 'plasmid' named entity '3CL protease' named entity '3C-like protease' named entity 'substrate' named entity 'molecular weight' named entity 'crystal structure' named entity 'peptide bond' named entity 'substrate' named entity 'hydrolyzed' named entity 'proteolysis' named entity 'LB medium' named entity 'incubation time' named entity 'Phe' named entity 'Escherichia coli' named entity 'substrate specificity' named entity 'proenzyme' named entity 'substrate' named entity 'peptide' named entity 'coronavirus' named entity 'SARS-CoV' named entity 'polyacrylamide gel electrophoresis' named entity 'SARS-CoV' named entity 'SARS-CoV' named entity 'CP2' named entity 'enzyme' named entity 'N-terminal' named entity 'highly conserved' named entity 'substrate specificities' named entity 'amino acids' named entity 'Gln' named entity 'proteases' named entity 'amino acids' named entity 'PCR' named entity 'Sub7'

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