Cloning, expression in Escherichia coli, and characterization of Arabidopsis thaliana UMP/CMP kinase
A cDNA encoding the Arabidopsis thaliana uridine 5'- monophosphate (UMP)/cytidine 5'-monophosphate (CMP) kinase was isolated by complementation of a Saccharomyces cerevisiae ura6 mutant. The deduced amino acid sequence of the plant UMP/CMP kinase has 50% identity with other eukaryotic UMP/...
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| Veröffentlicht in: | Plant physiology (Bethesda) 1998-05, Vol.117 (1), p.245-254 |
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| creator | Zhou, L. (Iowa State University, Ames, IA.) Lacroute, F Thornburg, R |
| description | A cDNA encoding the Arabidopsis thaliana uridine 5'- monophosphate (UMP)/cytidine 5'-monophosphate (CMP) kinase was isolated by complementation of a Saccharomyces cerevisiae ura6 mutant. The deduced amino acid sequence of the plant UMP/CMP kinase has 50% identity with other eukaryotic UMP/CMP kinase proteins. The cDNA was subcloned into pGEX-4T-3 and expressed as a glutathione S-transferase fusion protein in Escherichia coli. Following proteolytic digestion, the plant UMP/CMP kinase was purified and analyzed for its structural and kinetic properties. The mass, N-terminal sequence, and total amino acid composition agreed with the sequence and composition predicted from the cDNA sequence. Kinetic analysis revealed that the UMP/CMP kinase preferentially uses ATP (Michaelis constant [K(m)] = 29 micromolar when UMP is the other substrate and K(m) = 292 micromolar when CMP is the other substrate) as a phosphate donor. However, both UMP (K(m) = 153 micromolar) and CMP (K(m) = 266 micromolar) were equally acceptable as the phosphate acceptor. The optimal pH for the enzyme is 6.5. P1, P5-di(adenosine-5') pentaphosphate was found to be a competitive inhibitor of both ATP and UMP |
| doi_str_mv | 10.1104/pp.117.1.245 |
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(Iowa State University, Ames, IA.) ; Lacroute, F ; Thornburg, R</creator><creatorcontrib>Zhou, L. (Iowa State University, Ames, IA.) ; Lacroute, F ; Thornburg, R</creatorcontrib><description>A cDNA encoding the Arabidopsis thaliana uridine 5'- monophosphate (UMP)/cytidine 5'-monophosphate (CMP) kinase was isolated by complementation of a Saccharomyces cerevisiae ura6 mutant. The deduced amino acid sequence of the plant UMP/CMP kinase has 50% identity with other eukaryotic UMP/CMP kinase proteins. The cDNA was subcloned into pGEX-4T-3 and expressed as a glutathione S-transferase fusion protein in Escherichia coli. Following proteolytic digestion, the plant UMP/CMP kinase was purified and analyzed for its structural and kinetic properties. The mass, N-terminal sequence, and total amino acid composition agreed with the sequence and composition predicted from the cDNA sequence. Kinetic analysis revealed that the UMP/CMP kinase preferentially uses ATP (Michaelis constant [K(m)] = 29 micromolar when UMP is the other substrate and K(m) = 292 micromolar when CMP is the other substrate) as a phosphate donor. However, both UMP (K(m) = 153 micromolar) and CMP (K(m) = 266 micromolar) were equally acceptable as the phosphate acceptor. The optimal pH for the enzyme is 6.5. P1, P5-di(adenosine-5') pentaphosphate was found to be a competitive inhibitor of both ATP and UMP</description><identifier>ISSN: 0032-0889</identifier><identifier>EISSN: 1532-2548</identifier><identifier>DOI: 10.1104/pp.117.1.245</identifier><identifier>PMID: 9576794</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 ; Animals ; Arabidopsis - enzymology ; Arabidopsis - genetics ; ARABIDOPSIS THALIANA ; Base Sequence ; Biochemistry and Enzymology ; Biological and medical sciences ; CHEMICAL COMPOSITION ; CHEMICOPHYSICAL PROPERTIES ; CITIDINA ; CLONACION ; CLONAGE ; CLONING ; Cloning, Molecular ; CODE GENETIQUE ; CODIGO GENETICO ; Complementary DNA ; COMPOSICION QUIMICA ; COMPOSITION CHIMIQUE ; CYTIDINE ; CYTIDINE 5'-MONOPHOSPHATE ; DICTYOSTELIUM ; DICTYOSTELIUM DISCOIDEUM ; Dinucleoside Phosphates - pharmacology ; Enzyme Stability ; Enzymes ; Enzymes and enzyme inhibitors ; ENZYMIC ACTIVITY ; ESCHERICHIA COLI ; EXPRESION GENICA ; EXPRESSION DES GENES ; FOSFATOS ; Fundamental and applied biological sciences. Psychology ; GENBANK/AF000147 ; GENBANK/D29655 ; GENBANK/K02116 ; GENBANK/L04126 ; GENBANK/L16991 ; GENBANK/M34568 ; GENBANK/M69295 ; GENBANK/X78809 ; GENBANK/X83598 ; GENE ; GENE EXPRESSION ; GENE TRANSFER ; GENERO HUMANO ; GENES ; GENETIC CODE ; Genetic Complementation Test ; GENETIC REGULATION ; GENETICA ; GENETICS ; GENETIQUE ; GENRE HUMAIN ; Hydrogen-Ion Concentration ; Kinetics ; MANKIND ; Metabolism ; MOLECULAR SEQUENCE DATA ; Nucleoside-Phosphate Kinase - antagonists & inhibitors ; Nucleoside-Phosphate Kinase - chemistry ; Nucleoside-Phosphate Kinase - genetics ; NUCLEOTIDE ; NUCLEOTIDES ; NUCLEOTIDOS ; PHOSPHATE ; PHOSPHATES ; Plant physiology and development ; Plant Proteins - biosynthesis ; Plant Proteins - chemistry ; Plant Proteins - genetics ; PROPIEDADES FISICOQUIMICAS ; PROPRIETE PHYSICOCHIMIQUE ; PROTEINAS ; PROTEINE ; PROTEINS ; PURIFICACION ; PURIFICATION ; Pyrimidines ; RNA, Messenger - analysis ; SACCHAROMYCES CEREVISIAE ; SACCHAROMYCES POMBE ; SACCHAROMYCES SCROFA ; Sequence Alignment ; Sequence Homology, Amino Acid ; Substrate Specificity ; SUBSTRATES ; Swine ; Temperature ; THERMUS AQUATICUS ; TRANSFERASAS ; TRANSFERASE ; TRANSFERASES ; TRANSFERENCIA DE GENES ; TRANSFERT DE GENE ; Yeasts</subject><ispartof>Plant physiology (Bethesda), 1998-05, Vol.117 (1), p.245-254</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/4278274$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/4278274$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,777,781,800,882,27905,27906,57998,58231</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=2333715$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9576794$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhou, L. (Iowa State University, Ames, IA.)</creatorcontrib><creatorcontrib>Lacroute, F</creatorcontrib><creatorcontrib>Thornburg, R</creatorcontrib><title>Cloning, expression in Escherichia coli, and characterization of Arabidopsis thaliana UMP/CMP kinase</title><title>Plant physiology (Bethesda)</title><addtitle>Plant Physiol</addtitle><description>A cDNA encoding the Arabidopsis thaliana uridine 5'- monophosphate (UMP)/cytidine 5'-monophosphate (CMP) kinase was isolated by complementation of a Saccharomyces cerevisiae ura6 mutant. The deduced amino acid sequence of the plant UMP/CMP kinase has 50% identity with other eukaryotic UMP/CMP kinase proteins. The cDNA was subcloned into pGEX-4T-3 and expressed as a glutathione S-transferase fusion protein in Escherichia coli. Following proteolytic digestion, the plant UMP/CMP kinase was purified and analyzed for its structural and kinetic properties. The mass, N-terminal sequence, and total amino acid composition agreed with the sequence and composition predicted from the cDNA sequence. Kinetic analysis revealed that the UMP/CMP kinase preferentially uses ATP (Michaelis constant [K(m)] = 29 micromolar when UMP is the other substrate and K(m) = 292 micromolar when CMP is the other substrate) as a phosphate donor. However, both UMP (K(m) = 153 micromolar) and CMP (K(m) = 266 micromolar) were equally acceptable as the phosphate acceptor. The optimal pH for the enzyme is 6.5. P1, P5-di(adenosine-5') pentaphosphate was found to be a competitive inhibitor of both ATP and UMP</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>Animals</subject><subject>Arabidopsis - enzymology</subject><subject>Arabidopsis - genetics</subject><subject>ARABIDOPSIS THALIANA</subject><subject>Base Sequence</subject><subject>Biochemistry and Enzymology</subject><subject>Biological and medical sciences</subject><subject>CHEMICAL COMPOSITION</subject><subject>CHEMICOPHYSICAL PROPERTIES</subject><subject>CITIDINA</subject><subject>CLONACION</subject><subject>CLONAGE</subject><subject>CLONING</subject><subject>Cloning, Molecular</subject><subject>CODE GENETIQUE</subject><subject>CODIGO GENETICO</subject><subject>Complementary DNA</subject><subject>COMPOSICION QUIMICA</subject><subject>COMPOSITION CHIMIQUE</subject><subject>CYTIDINE</subject><subject>CYTIDINE 5'-MONOPHOSPHATE</subject><subject>DICTYOSTELIUM</subject><subject>DICTYOSTELIUM DISCOIDEUM</subject><subject>Dinucleoside Phosphates - pharmacology</subject><subject>Enzyme Stability</subject><subject>Enzymes</subject><subject>Enzymes and enzyme inhibitors</subject><subject>ENZYMIC ACTIVITY</subject><subject>ESCHERICHIA COLI</subject><subject>EXPRESION GENICA</subject><subject>EXPRESSION DES GENES</subject><subject>FOSFATOS</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>GENBANK/AF000147</subject><subject>GENBANK/D29655</subject><subject>GENBANK/K02116</subject><subject>GENBANK/L04126</subject><subject>GENBANK/L16991</subject><subject>GENBANK/M34568</subject><subject>GENBANK/M69295</subject><subject>GENBANK/X78809</subject><subject>GENBANK/X83598</subject><subject>GENE</subject><subject>GENE EXPRESSION</subject><subject>GENE TRANSFER</subject><subject>GENERO HUMANO</subject><subject>GENES</subject><subject>GENETIC CODE</subject><subject>Genetic Complementation Test</subject><subject>GENETIC REGULATION</subject><subject>GENETICA</subject><subject>GENETICS</subject><subject>GENETIQUE</subject><subject>GENRE HUMAIN</subject><subject>Hydrogen-Ion Concentration</subject><subject>Kinetics</subject><subject>MANKIND</subject><subject>Metabolism</subject><subject>MOLECULAR SEQUENCE DATA</subject><subject>Nucleoside-Phosphate Kinase - antagonists & inhibitors</subject><subject>Nucleoside-Phosphate Kinase - chemistry</subject><subject>Nucleoside-Phosphate Kinase - genetics</subject><subject>NUCLEOTIDE</subject><subject>NUCLEOTIDES</subject><subject>NUCLEOTIDOS</subject><subject>PHOSPHATE</subject><subject>PHOSPHATES</subject><subject>Plant physiology and development</subject><subject>Plant Proteins - biosynthesis</subject><subject>Plant Proteins - chemistry</subject><subject>Plant Proteins - genetics</subject><subject>PROPIEDADES FISICOQUIMICAS</subject><subject>PROPRIETE PHYSICOCHIMIQUE</subject><subject>PROTEINAS</subject><subject>PROTEINE</subject><subject>PROTEINS</subject><subject>PURIFICACION</subject><subject>PURIFICATION</subject><subject>Pyrimidines</subject><subject>RNA, Messenger - analysis</subject><subject>SACCHAROMYCES CEREVISIAE</subject><subject>SACCHAROMYCES POMBE</subject><subject>SACCHAROMYCES SCROFA</subject><subject>Sequence Alignment</subject><subject>Sequence Homology, Amino Acid</subject><subject>Substrate Specificity</subject><subject>SUBSTRATES</subject><subject>Swine</subject><subject>Temperature</subject><subject>THERMUS AQUATICUS</subject><subject>TRANSFERASAS</subject><subject>TRANSFERASE</subject><subject>TRANSFERASES</subject><subject>TRANSFERENCIA DE GENES</subject><subject>TRANSFERT DE GENE</subject><subject>Yeasts</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>eNqFkU2LFDEQhoMo6zh686iQg3jamc1nJwEvy7B-wC4u6Jyb6iQ9nbUnaZMeUX-9kR1GPXmqguepqpcEoeeUrCkl4mKaalVrumZCPkALKjlbMSn0Q7QgpPZEa_MYPSnljhBCORVn6MxI1SgjFshtxhRD3J1j_33KvpSQIg4RXxU7-BzsEADbNIZzDNFhO0AGO1fwE-bfZurxZYYuuDSVUPA8wBggAt7e3F5sbm7xlxCh-KfoUQ9j8c-OdYm2b68-b96vrj---7C5vF713Oh5xTXpKFM9sw4ao7gBYxqljZFed07X7M53vGl0LyiFTjTSOyENNJR2xvUdX6I393unQ7f3zvo4ZxjbKYc95B9tgtD-S2IY2l361nJJiKnjr4_jOX09-DK3-1CsH0eIPh1Kq4yWRjfqvyJVTHJBeBVf_h3olOT4_JW_OnIoFsY-Q7ShnDTGOVf1P5foxb12V-aUT1gwpZkSf670kFrY5bph-4kao4hhNTL_BZjLpqQ</recordid><startdate>19980501</startdate><enddate>19980501</enddate><creator>Zhou, L. (Iowa State University, Ames, IA.)</creator><creator>Lacroute, F</creator><creator>Thornburg, R</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>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19980501</creationdate><title>Cloning, expression in Escherichia coli, and characterization of Arabidopsis thaliana UMP/CMP kinase</title><author>Zhou, L. (Iowa State University, Ames, IA.) ; Lacroute, F ; Thornburg, R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-f398t-380b127f2cda69739a99678995e8bd8013deb3668f411ab465ed459a611b9dfb3</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>Animals</topic><topic>Arabidopsis - enzymology</topic><topic>Arabidopsis - genetics</topic><topic>ARABIDOPSIS THALIANA</topic><topic>Base Sequence</topic><topic>Biochemistry and Enzymology</topic><topic>Biological and medical sciences</topic><topic>CHEMICAL COMPOSITION</topic><topic>CHEMICOPHYSICAL PROPERTIES</topic><topic>CITIDINA</topic><topic>CLONACION</topic><topic>CLONAGE</topic><topic>CLONING</topic><topic>Cloning, Molecular</topic><topic>CODE GENETIQUE</topic><topic>CODIGO GENETICO</topic><topic>Complementary DNA</topic><topic>COMPOSICION QUIMICA</topic><topic>COMPOSITION CHIMIQUE</topic><topic>CYTIDINE</topic><topic>CYTIDINE 5'-MONOPHOSPHATE</topic><topic>DICTYOSTELIUM</topic><topic>DICTYOSTELIUM DISCOIDEUM</topic><topic>Dinucleoside Phosphates - pharmacology</topic><topic>Enzyme Stability</topic><topic>Enzymes</topic><topic>Enzymes and enzyme inhibitors</topic><topic>ENZYMIC ACTIVITY</topic><topic>ESCHERICHIA COLI</topic><topic>EXPRESION GENICA</topic><topic>EXPRESSION DES GENES</topic><topic>FOSFATOS</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>GENBANK/AF000147</topic><topic>GENBANK/D29655</topic><topic>GENBANK/K02116</topic><topic>GENBANK/L04126</topic><topic>GENBANK/L16991</topic><topic>GENBANK/M34568</topic><topic>GENBANK/M69295</topic><topic>GENBANK/X78809</topic><topic>GENBANK/X83598</topic><topic>GENE</topic><topic>GENE EXPRESSION</topic><topic>GENE TRANSFER</topic><topic>GENERO HUMANO</topic><topic>GENES</topic><topic>GENETIC CODE</topic><topic>Genetic Complementation Test</topic><topic>GENETIC REGULATION</topic><topic>GENETICA</topic><topic>GENETICS</topic><topic>GENETIQUE</topic><topic>GENRE HUMAIN</topic><topic>Hydrogen-Ion Concentration</topic><topic>Kinetics</topic><topic>MANKIND</topic><topic>Metabolism</topic><topic>MOLECULAR SEQUENCE DATA</topic><topic>Nucleoside-Phosphate Kinase - antagonists & inhibitors</topic><topic>Nucleoside-Phosphate Kinase - chemistry</topic><topic>Nucleoside-Phosphate Kinase - genetics</topic><topic>NUCLEOTIDE</topic><topic>NUCLEOTIDES</topic><topic>NUCLEOTIDOS</topic><topic>PHOSPHATE</topic><topic>PHOSPHATES</topic><topic>Plant physiology and development</topic><topic>Plant Proteins - biosynthesis</topic><topic>Plant Proteins - chemistry</topic><topic>Plant Proteins - genetics</topic><topic>PROPIEDADES FISICOQUIMICAS</topic><topic>PROPRIETE PHYSICOCHIMIQUE</topic><topic>PROTEINAS</topic><topic>PROTEINE</topic><topic>PROTEINS</topic><topic>PURIFICACION</topic><topic>PURIFICATION</topic><topic>Pyrimidines</topic><topic>RNA, Messenger - analysis</topic><topic>SACCHAROMYCES CEREVISIAE</topic><topic>SACCHAROMYCES POMBE</topic><topic>SACCHAROMYCES SCROFA</topic><topic>Sequence Alignment</topic><topic>Sequence Homology, Amino Acid</topic><topic>Substrate Specificity</topic><topic>SUBSTRATES</topic><topic>Swine</topic><topic>Temperature</topic><topic>THERMUS AQUATICUS</topic><topic>TRANSFERASAS</topic><topic>TRANSFERASE</topic><topic>TRANSFERASES</topic><topic>TRANSFERENCIA DE GENES</topic><topic>TRANSFERT DE GENE</topic><topic>Yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zhou, L. (Iowa State University, Ames, IA.)</creatorcontrib><creatorcontrib>Lacroute, F</creatorcontrib><creatorcontrib>Thornburg, R</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>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</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>Zhou, L. (Iowa State University, Ames, IA.)</au><au>Lacroute, F</au><au>Thornburg, R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cloning, expression in Escherichia coli, and characterization of Arabidopsis thaliana UMP/CMP kinase</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>245</spage><epage>254</epage><pages>245-254</pages><issn>0032-0889</issn><eissn>1532-2548</eissn><coden>PPHYA5</coden><abstract>A cDNA encoding the Arabidopsis thaliana uridine 5'- monophosphate (UMP)/cytidine 5'-monophosphate (CMP) kinase was isolated by complementation of a Saccharomyces cerevisiae ura6 mutant. The deduced amino acid sequence of the plant UMP/CMP kinase has 50% identity with other eukaryotic UMP/CMP kinase proteins. The cDNA was subcloned into pGEX-4T-3 and expressed as a glutathione S-transferase fusion protein in Escherichia coli. Following proteolytic digestion, the plant UMP/CMP kinase was purified and analyzed for its structural and kinetic properties. The mass, N-terminal sequence, and total amino acid composition agreed with the sequence and composition predicted from the cDNA sequence. Kinetic analysis revealed that the UMP/CMP kinase preferentially uses ATP (Michaelis constant [K(m)] = 29 micromolar when UMP is the other substrate and K(m) = 292 micromolar when CMP is the other substrate) as a phosphate donor. However, both UMP (K(m) = 153 micromolar) and CMP (K(m) = 266 micromolar) were equally acceptable as the phosphate acceptor. The optimal pH for the enzyme is 6.5. P1, P5-di(adenosine-5') pentaphosphate was found to be a competitive inhibitor of both ATP and UMP</abstract><cop>Rockville, MD</cop><pub>American Society of Plant Physiologists</pub><pmid>9576794</pmid><doi>10.1104/pp.117.1.245</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0032-0889 |
| ispartof | Plant physiology (Bethesda), 1998-05, Vol.117 (1), p.245-254 |
| issn | 0032-0889 1532-2548 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_79859867 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Jstor Complete Legacy; Oxford University Press Journals All Titles (1996-Current) |
| subjects | ACTIVIDAD ENZIMATICA ACTIVITE ENZYMATIQUE Amino Acid Sequence AMINO ACID SEQUENCES Amino acids Analytical, structural and metabolic biochemistry Animals Arabidopsis - enzymology Arabidopsis - genetics ARABIDOPSIS THALIANA Base Sequence Biochemistry and Enzymology Biological and medical sciences CHEMICAL COMPOSITION CHEMICOPHYSICAL PROPERTIES CITIDINA CLONACION CLONAGE CLONING Cloning, Molecular CODE GENETIQUE CODIGO GENETICO Complementary DNA COMPOSICION QUIMICA COMPOSITION CHIMIQUE CYTIDINE CYTIDINE 5'-MONOPHOSPHATE DICTYOSTELIUM DICTYOSTELIUM DISCOIDEUM Dinucleoside Phosphates - pharmacology Enzyme Stability Enzymes Enzymes and enzyme inhibitors ENZYMIC ACTIVITY ESCHERICHIA COLI EXPRESION GENICA EXPRESSION DES GENES FOSFATOS Fundamental and applied biological sciences. Psychology GENBANK/AF000147 GENBANK/D29655 GENBANK/K02116 GENBANK/L04126 GENBANK/L16991 GENBANK/M34568 GENBANK/M69295 GENBANK/X78809 GENBANK/X83598 GENE GENE EXPRESSION GENE TRANSFER GENERO HUMANO GENES GENETIC CODE Genetic Complementation Test GENETIC REGULATION GENETICA GENETICS GENETIQUE GENRE HUMAIN Hydrogen-Ion Concentration Kinetics MANKIND Metabolism MOLECULAR SEQUENCE DATA Nucleoside-Phosphate Kinase - antagonists & inhibitors Nucleoside-Phosphate Kinase - chemistry Nucleoside-Phosphate Kinase - genetics NUCLEOTIDE NUCLEOTIDES NUCLEOTIDOS PHOSPHATE PHOSPHATES Plant physiology and development Plant Proteins - biosynthesis Plant Proteins - chemistry Plant Proteins - genetics PROPIEDADES FISICOQUIMICAS PROPRIETE PHYSICOCHIMIQUE PROTEINAS PROTEINE PROTEINS PURIFICACION PURIFICATION Pyrimidines RNA, Messenger - analysis SACCHAROMYCES CEREVISIAE SACCHAROMYCES POMBE SACCHAROMYCES SCROFA Sequence Alignment Sequence Homology, Amino Acid Substrate Specificity SUBSTRATES Swine Temperature THERMUS AQUATICUS TRANSFERASAS TRANSFERASE TRANSFERASES TRANSFERENCIA DE GENES TRANSFERT DE GENE Yeasts |
| title | Cloning, expression in Escherichia coli, and characterization of Arabidopsis thaliana UMP/CMP kinase |
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