Substrate specificity of barley cysteine endoproteases EP-A and EP-B
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,...
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| Veröffentlicht in: | Plant physiology (Bethesda) 1998-05, Vol.117 (1), p.255-261 |
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| creator | Davy, A. (Carlsberg Research Laboratory, Denmark.) Svendsen, I Sorensen, S.O Sorensen, M.B Rouster, J Meldal, M Simpson, D.J Cameron-Mills, V |
| description | 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 K(m) values |
| doi_str_mv | 10.1104/pp.117.1.255 |
| format | Article |
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(Carlsberg Research Laboratory, Denmark.) ; Svendsen, I ; Sorensen, S.O ; Sorensen, M.B ; Rouster, J ; Meldal, M ; Simpson, D.J ; Cameron-Mills, V</creator><creatorcontrib>Davy, A. (Carlsberg Research Laboratory, Denmark.) ; Svendsen, I ; Sorensen, S.O ; Sorensen, M.B ; Rouster, J ; Meldal, M ; Simpson, D.J ; Cameron-Mills, V</creatorcontrib><description>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 K(m) values</description><identifier>ISSN: 0032-0889</identifier><identifier>EISSN: 1532-2548</identifier><identifier>DOI: 10.1104/pp.117.1.255</identifier><identifier>PMID: 9576795</identifier><identifier>CODEN: PPHYA5</identifier><language>eng</language><publisher>Rockville, MD: American Society of Plant Physiologists</publisher><subject>ACTIVIDAD ENZIMATICA ; ACTIVITE ENZYMATIQUE ; Amino Acid Sequence ; AMINO ACID SEQUENCES ; Amino acids ; Analytical, structural and metabolic biochemistry ; ARGININA ; ARGININE ; Barley ; Binding Sites ; Biochemistry and Enzymology ; Biological and medical sciences ; CHEMICAL COMPOSITION ; CHEMICAL REACTIONS ; Chromogenic Compounds - metabolism ; COMPOSICION APROXIMADA ; COMPOSICION QUIMICA ; COMPOSITION CHIMIQUE ; COMPOSITION GLOBALE ; Cysteine Endopeptidases - genetics ; Cysteine Endopeptidases - isolation & purification ; Cysteine Endopeptidases - metabolism ; CYSTEINE PROTEINASES ; DEGRADACION ; DEGRADATION ; ENDOSPERM ; ENDOSPERMA ; ENDOSPERME ; Enzyme Activation ; Enzyme substrates ; Enzymes ; Enzymes and enzyme inhibitors ; ENZYMIC ACTIVITY ; FENILALANINA ; FOOD COMPOSITION ; Fundamental and applied biological sciences. Psychology ; Gels ; GLUTAMINA ; GLUTAMINE ; Glutens ; HORDEIN ; Hordeum - enzymology ; Hordeum - genetics ; HORDEUM VULGARE ; Hydrolases ; Hydrolysis ; KINETICS ; LEUCINA ; LEUCINE ; MALT ; MALTA (PRODUCTO) ; Metabolism ; MOLECULAR SEQUENCE DATA ; Molecular Weight ; Mutagenesis, Site-Directed ; PAPAIN ; PAPAINA ; PAPAINE ; PHENYLALANINE ; Plant physiology and development ; Plant Proteins - genetics ; Plant Proteins - metabolism ; PROLAMINAS ; PROLAMINE ; PROLAMINES ; PROLINA ; PROLINE ; PROTEASAS ; PROTEASE ; PROTEASES ; PROTEINAS ; PROTEINE ; PROTEINS ; PROXIMATE COMPOSITION ; REACCIONES QUIMICAS ; REACTION CHIMIQUE ; Sequencing ; Site directed mutagenesis ; Substrate Specificity ; VALINA ; VALINE</subject><ispartof>Plant physiology (Bethesda), 1998-05, Vol.117 (1), p.255-261</ispartof><rights>Copyright 1998 American Society of Plant Physiologists</rights><rights>1998 INIST-CNRS</rights><rights>1998</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/4278275$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/4278275$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,780,784,803,885,27922,27923,58015,58248</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=2333432$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9576795$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Davy, A. (Carlsberg Research Laboratory, Denmark.)</creatorcontrib><creatorcontrib>Svendsen, I</creatorcontrib><creatorcontrib>Sorensen, S.O</creatorcontrib><creatorcontrib>Sorensen, M.B</creatorcontrib><creatorcontrib>Rouster, J</creatorcontrib><creatorcontrib>Meldal, M</creatorcontrib><creatorcontrib>Simpson, D.J</creatorcontrib><creatorcontrib>Cameron-Mills, V</creatorcontrib><title>Substrate specificity of barley cysteine endoproteases EP-A and EP-B</title><title>Plant physiology (Bethesda)</title><addtitle>Plant Physiol</addtitle><description>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 K(m) values</description><subject>ACTIVIDAD ENZIMATICA</subject><subject>ACTIVITE ENZYMATIQUE</subject><subject>Amino Acid Sequence</subject><subject>AMINO ACID SEQUENCES</subject><subject>Amino acids</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>ARGININA</subject><subject>ARGININE</subject><subject>Barley</subject><subject>Binding Sites</subject><subject>Biochemistry and Enzymology</subject><subject>Biological and medical sciences</subject><subject>CHEMICAL COMPOSITION</subject><subject>CHEMICAL REACTIONS</subject><subject>Chromogenic Compounds - metabolism</subject><subject>COMPOSICION APROXIMADA</subject><subject>COMPOSICION QUIMICA</subject><subject>COMPOSITION CHIMIQUE</subject><subject>COMPOSITION GLOBALE</subject><subject>Cysteine Endopeptidases - genetics</subject><subject>Cysteine Endopeptidases - isolation & purification</subject><subject>Cysteine Endopeptidases - metabolism</subject><subject>CYSTEINE PROTEINASES</subject><subject>DEGRADACION</subject><subject>DEGRADATION</subject><subject>ENDOSPERM</subject><subject>ENDOSPERMA</subject><subject>ENDOSPERME</subject><subject>Enzyme Activation</subject><subject>Enzyme substrates</subject><subject>Enzymes</subject><subject>Enzymes and enzyme inhibitors</subject><subject>ENZYMIC ACTIVITY</subject><subject>FENILALANINA</subject><subject>FOOD COMPOSITION</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gels</subject><subject>GLUTAMINA</subject><subject>GLUTAMINE</subject><subject>Glutens</subject><subject>HORDEIN</subject><subject>Hordeum - enzymology</subject><subject>Hordeum - genetics</subject><subject>HORDEUM VULGARE</subject><subject>Hydrolases</subject><subject>Hydrolysis</subject><subject>KINETICS</subject><subject>LEUCINA</subject><subject>LEUCINE</subject><subject>MALT</subject><subject>MALTA (PRODUCTO)</subject><subject>Metabolism</subject><subject>MOLECULAR SEQUENCE DATA</subject><subject>Molecular Weight</subject><subject>Mutagenesis, Site-Directed</subject><subject>PAPAIN</subject><subject>PAPAINA</subject><subject>PAPAINE</subject><subject>PHENYLALANINE</subject><subject>Plant physiology and development</subject><subject>Plant Proteins - genetics</subject><subject>Plant Proteins - metabolism</subject><subject>PROLAMINAS</subject><subject>PROLAMINE</subject><subject>PROLAMINES</subject><subject>PROLINA</subject><subject>PROLINE</subject><subject>PROTEASAS</subject><subject>PROTEASE</subject><subject>PROTEASES</subject><subject>PROTEINAS</subject><subject>PROTEINE</subject><subject>PROTEINS</subject><subject>PROXIMATE COMPOSITION</subject><subject>REACCIONES QUIMICAS</subject><subject>REACTION CHIMIQUE</subject><subject>Sequencing</subject><subject>Site directed mutagenesis</subject><subject>Substrate Specificity</subject><subject>VALINA</subject><subject>VALINE</subject><issn>0032-0889</issn><issn>1532-2548</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVUEtLAzEQDqLUWr15VNiD163JJtkk4EVrfUBBofa8zOZRU9rdJdkK--9daak6l--D7zHDIHRJ8JgQzG6bpkcxJuOM8yM0JJxmacaZPEZDjHuOpVSn6CzGFcaYUMIGaKC4yIXiQ_Q435axDdDaJDZWe-e1b7ukdkkJYW27RHextb6yia1M3YS6tRBtTKbv6X0ClfkhD-foxME62os9jtDiafoxeUlnb8-vk_tZ6mgu2lTnjonSGMpzR0WugBjmCAiBMegSa3ACsCq5ZFIabo0TPJeuH4GdEaWiI3S362225cYabav-8nXRBL-B0BU1-OK_UvnPYll_FZRjgvv49d_4Ibd_Rq_f7HWIGtYuQKV9PNgySimjWW-72tlWsa3DQWaZkJngv1sc1AUsQ9-wmBOlBFaZkoJ-AyezgVM</recordid><startdate>19980501</startdate><enddate>19980501</enddate><creator>Davy, A. (Carlsberg Research Laboratory, Denmark.)</creator><creator>Svendsen, I</creator><creator>Sorensen, S.O</creator><creator>Sorensen, M.B</creator><creator>Rouster, J</creator><creator>Meldal, M</creator><creator>Simpson, D.J</creator><creator>Cameron-Mills, V</creator><general>American Society of Plant Physiologists</general><scope>FBQ</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>5PM</scope></search><sort><creationdate>19980501</creationdate><title>Substrate specificity of barley cysteine endoproteases EP-A and EP-B</title><author>Davy, A. (Carlsberg Research Laboratory, Denmark.) ; Svendsen, I ; Sorensen, S.O ; Sorensen, M.B ; Rouster, J ; Meldal, M ; Simpson, D.J ; Cameron-Mills, V</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-f367t-c6f47bdd356f3769a1d4f1a7700acb0caf7a09b58488d5edf7568ffff70fd7b93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>ACTIVIDAD ENZIMATICA</topic><topic>ACTIVITE ENZYMATIQUE</topic><topic>Amino Acid Sequence</topic><topic>AMINO ACID SEQUENCES</topic><topic>Amino acids</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>ARGININA</topic><topic>ARGININE</topic><topic>Barley</topic><topic>Binding Sites</topic><topic>Biochemistry and Enzymology</topic><topic>Biological and medical sciences</topic><topic>CHEMICAL COMPOSITION</topic><topic>CHEMICAL REACTIONS</topic><topic>Chromogenic Compounds - metabolism</topic><topic>COMPOSICION APROXIMADA</topic><topic>COMPOSICION QUIMICA</topic><topic>COMPOSITION CHIMIQUE</topic><topic>COMPOSITION GLOBALE</topic><topic>Cysteine Endopeptidases - genetics</topic><topic>Cysteine Endopeptidases - isolation & purification</topic><topic>Cysteine Endopeptidases - metabolism</topic><topic>CYSTEINE PROTEINASES</topic><topic>DEGRADACION</topic><topic>DEGRADATION</topic><topic>ENDOSPERM</topic><topic>ENDOSPERMA</topic><topic>ENDOSPERME</topic><topic>Enzyme Activation</topic><topic>Enzyme substrates</topic><topic>Enzymes</topic><topic>Enzymes and enzyme inhibitors</topic><topic>ENZYMIC ACTIVITY</topic><topic>FENILALANINA</topic><topic>FOOD COMPOSITION</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gels</topic><topic>GLUTAMINA</topic><topic>GLUTAMINE</topic><topic>Glutens</topic><topic>HORDEIN</topic><topic>Hordeum - enzymology</topic><topic>Hordeum - genetics</topic><topic>HORDEUM VULGARE</topic><topic>Hydrolases</topic><topic>Hydrolysis</topic><topic>KINETICS</topic><topic>LEUCINA</topic><topic>LEUCINE</topic><topic>MALT</topic><topic>MALTA (PRODUCTO)</topic><topic>Metabolism</topic><topic>MOLECULAR SEQUENCE DATA</topic><topic>Molecular Weight</topic><topic>Mutagenesis, Site-Directed</topic><topic>PAPAIN</topic><topic>PAPAINA</topic><topic>PAPAINE</topic><topic>PHENYLALANINE</topic><topic>Plant physiology and development</topic><topic>Plant Proteins - genetics</topic><topic>Plant Proteins - metabolism</topic><topic>PROLAMINAS</topic><topic>PROLAMINE</topic><topic>PROLAMINES</topic><topic>PROLINA</topic><topic>PROLINE</topic><topic>PROTEASAS</topic><topic>PROTEASE</topic><topic>PROTEASES</topic><topic>PROTEINAS</topic><topic>PROTEINE</topic><topic>PROTEINS</topic><topic>PROXIMATE COMPOSITION</topic><topic>REACCIONES QUIMICAS</topic><topic>REACTION CHIMIQUE</topic><topic>Sequencing</topic><topic>Site directed mutagenesis</topic><topic>Substrate Specificity</topic><topic>VALINA</topic><topic>VALINE</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Davy, A. (Carlsberg Research Laboratory, Denmark.)</creatorcontrib><creatorcontrib>Svendsen, I</creatorcontrib><creatorcontrib>Sorensen, S.O</creatorcontrib><creatorcontrib>Sorensen, M.B</creatorcontrib><creatorcontrib>Rouster, J</creatorcontrib><creatorcontrib>Meldal, M</creatorcontrib><creatorcontrib>Simpson, D.J</creatorcontrib><creatorcontrib>Cameron-Mills, V</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Plant physiology (Bethesda)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Davy, A. (Carlsberg Research Laboratory, Denmark.)</au><au>Svendsen, I</au><au>Sorensen, S.O</au><au>Sorensen, M.B</au><au>Rouster, J</au><au>Meldal, M</au><au>Simpson, D.J</au><au>Cameron-Mills, V</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Substrate specificity of barley cysteine endoproteases EP-A and EP-B</atitle><jtitle>Plant physiology (Bethesda)</jtitle><addtitle>Plant Physiol</addtitle><date>1998-05-01</date><risdate>1998</risdate><volume>117</volume><issue>1</issue><spage>255</spage><epage>261</epage><pages>255-261</pages><issn>0032-0889</issn><eissn>1532-2548</eissn><coden>PPHYA5</coden><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 K(m) values</abstract><cop>Rockville, MD</cop><pub>American Society of Plant Physiologists</pub><pmid>9576795</pmid><doi>10.1104/pp.117.1.255</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Plant physiology (Bethesda), 1998-05, Vol.117 (1), p.255-261 |
| issn | 0032-0889 1532-2548 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_35010 |
| source | MEDLINE; JSTOR Archive Collection A-Z Listing; Oxford University Press Journals All Titles (1996-Current); EZB-FREE-00999 freely available EZB journals |
| subjects | ACTIVIDAD ENZIMATICA ACTIVITE ENZYMATIQUE Amino Acid Sequence AMINO ACID SEQUENCES Amino acids Analytical, structural and metabolic biochemistry ARGININA ARGININE Barley Binding Sites Biochemistry and Enzymology Biological and medical sciences CHEMICAL COMPOSITION CHEMICAL REACTIONS Chromogenic Compounds - metabolism COMPOSICION APROXIMADA COMPOSICION QUIMICA COMPOSITION CHIMIQUE COMPOSITION GLOBALE Cysteine Endopeptidases - genetics Cysteine Endopeptidases - isolation & purification Cysteine Endopeptidases - metabolism CYSTEINE PROTEINASES DEGRADACION DEGRADATION ENDOSPERM ENDOSPERMA ENDOSPERME Enzyme Activation Enzyme substrates Enzymes Enzymes and enzyme inhibitors ENZYMIC ACTIVITY FENILALANINA FOOD COMPOSITION Fundamental and applied biological sciences. Psychology Gels GLUTAMINA GLUTAMINE Glutens HORDEIN Hordeum - enzymology Hordeum - genetics HORDEUM VULGARE Hydrolases Hydrolysis KINETICS LEUCINA LEUCINE MALT MALTA (PRODUCTO) Metabolism MOLECULAR SEQUENCE DATA Molecular Weight Mutagenesis, Site-Directed PAPAIN PAPAINA PAPAINE PHENYLALANINE Plant physiology and development Plant Proteins - genetics Plant Proteins - metabolism PROLAMINAS PROLAMINE PROLAMINES PROLINA PROLINE PROTEASAS PROTEASE PROTEASES PROTEINAS PROTEINE PROTEINS PROXIMATE COMPOSITION REACCIONES QUIMICAS REACTION CHIMIQUE Sequencing Site directed mutagenesis Substrate Specificity VALINA VALINE |
| title | Substrate specificity of barley cysteine endoproteases EP-A and EP-B |
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