ArticlePlant physiology1998
Substrate specificity of barley cysteine endoproteases EP-A and EP-B.
Article in Plant physiology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 52 citations in OpenAlex.
- Mycotoxins from Fusarium proliferatum: new inhibitors of papain-like cysteine proteases.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2020Article
- Targeted modification of wheat grain protein to reduce the content of celiac causing epitopes.Functional & integrative genomics · 2012Review
- Oral enzyme therapy for celiac sprue.Methods in enzymology · 2012Article
- Characterization of the entire cystatin gene family in barley and their target cathepsin L-like cysteine-proteases, partners in the hordein mobilization during seed germination.Plant physiology · 2009Article
- Cloning and characterization of a novel cysteine protease gene (HbCP1) from Hevea brasiliensis.Journal of biosciences · 2008Article
- Identification, cDNA cloning and possible roles of seed-specific rice asparaginyl endopeptidase, REP-2.Planta · 2003Article
- Ara12 subtilisin-like protease from Arabidopsis thaliana: purification, substrate specificity and tissue localization.The Biochemical journal · 2003Article
- Purification and characterization of barley dipeptidyl peptidase IV.Plant physiology · 2000Article
- Prediction of protein cleavage sites by the barley cysteine endoproteases EP-A and EP-B based on the kinetics of synthetic peptide hydrolysis.Plant physiology · 2000Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The cysteine endoproteases (EP)-A and EP-B were purified from green barley (Hordeum vulgare L.) malt, and their identity was confirmed by N-terminal amino acid sequencing. EP-B cleavage sites in recombinant type-C hordein were determined by N-terminal amino acid sequencing of the cleavage products, and were used to design internally quenched, fluorogenic peptide substrates. Tetrapeptide substrates of the general formula 2-aminobenzoyl-P2-P1-P1'-P2'-tyrosine(NO2)-aspartic acid, in which cleavage occurs between P1 and P1', showed that the cysteine EPs preferred phenylalanine, leucine, or valine at P2. Arginine was preferred to glutamine at P1, whereas proline at P2, P1, or P1' greatly reduced substrate kinetic specificity. Enzyme cleavage of C hordein was mainly determined by the primary sequence at the cleavage site, because elongation of substrates, based on the C hordein sequence, did not make them more suitable substrates. Site-directed mutagenesis of C hordein, in which serine or proline replaced leucine, destroyed primary cleavage sites. EP-A and EP-B were both more active than papain, mostly because of their much lower Km values.
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