Purification, characterization, and gene cloning of glucose-1-phosphatase from Citrobacter braakii
Citrobacter braakii produced an intracellular acid glucose phosphatase (AgpC) which was purified 986 fold to homogeneity with the specific activity of 286 units/mg. AgpC hydrolyzed a wide variety of phosphorylated compounds with high activity for glucose-1-phosphate and glucose-6-phosphate. The opti...
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| Veröffentlicht in: | Journal of general and applied microbiology 2009, Vol.55(5), pp.345-350 |
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| creator | Kim, Young-Ok Kim, Han-Woo Park, In-Suk Lee, Jeong-Ho Lee, Sang-Jun Kim, Kyung-Kil |
| description | Citrobacter braakii produced an intracellular acid glucose phosphatase (AgpC) which was purified 986 fold to homogeneity with the specific activity of 286 units/mg. AgpC hydrolyzed a wide variety of phosphorylated compounds with high activity for glucose-1-phosphate and glucose-6-phosphate. The optimum pH and temperature for the enzyme activity was pH 5.0 and 45°C, respectively. The Km value for glucose-1-phosphate was 5.12 mM with a Vmax 27.8 U mg-1. Its molecular weight was 46 kDa by SDS-PAGE gel and the sequence of N-terminal amino acid residues identified was Gln-Thr-Ala-Pro-Glu-Gly-Tyr-Gln-Leu-Gln. The glucose-1-phosphatase gene (agpC) was cloned from the C. braakii genomic library. This gene comprised 1,242 nucleotides and encoded a polypeptide of 413 amino acids. The result of its BLAST search showed a significant similarity with glucose-1-phosphatase from enterobacteria such as E. coli, Enterobacter, Shigella, and Salmonella. |
| doi_str_mv | 10.2323/jgam.55.345 |
| format | Article |
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AgpC hydrolyzed a wide variety of phosphorylated compounds with high activity for glucose-1-phosphate and glucose-6-phosphate. The optimum pH and temperature for the enzyme activity was pH 5.0 and 45°C, respectively. The Km value for glucose-1-phosphate was 5.12 mM with a Vmax 27.8 U mg-1. Its molecular weight was 46 kDa by SDS-PAGE gel and the sequence of N-terminal amino acid residues identified was Gln-Thr-Ala-Pro-Glu-Gly-Tyr-Gln-Leu-Gln. The glucose-1-phosphatase gene (agpC) was cloned from the C. braakii genomic library. This gene comprised 1,242 nucleotides and encoded a polypeptide of 413 amino acids. The result of its BLAST search showed a significant similarity with glucose-1-phosphatase from enterobacteria such as E. coli, Enterobacter, Shigella, and Salmonella.</description><identifier>ISSN: 0022-1260</identifier><identifier>EISSN: 1349-8037</identifier><identifier>DOI: 10.2323/jgam.55.345</identifier><identifier>PMID: 19940380</identifier><language>eng</language><publisher>Japan: Applied Microbiology, Molecular and Cellular Biosciences Research Foundation</publisher><subject>Amino Acid Sequence ; Citrobacter ; Citrobacter - chemistry ; Citrobacter - genetics ; Citrobacter - isolation & purification ; Citrobacter braakii ; cloning ; Cloning, Molecular ; Dipeptides - analysis ; Enterobacter ; Escherichia coli ; glucose-1-phosphatase ; Glucosephosphates - analysis ; Molecular Sequence Data ; Peptide Fragments ; Phylogeny ; Protein Conformation ; Salmonella ; Shigella ; substrate specificity</subject><ispartof>The Journal of General and Applied Microbiology, 2009, Vol.55(5), pp.345-350</ispartof><rights>2009 by The Applied Microbiology, Molecular and Cellular Biosciences Research Foundation</rights><rights>Copyright Japan Science and Technology Agency 2009</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c564t-a95a6eff0ac5292d4ff0a63b109d56b7d86013067359f6f3b91c2f37006584313</citedby><cites>FETCH-LOGICAL-c564t-a95a6eff0ac5292d4ff0a63b109d56b7d86013067359f6f3b91c2f37006584313</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,1876,4009,27902,27903,27904</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19940380$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kim, Young-Ok</creatorcontrib><creatorcontrib>Kim, Han-Woo</creatorcontrib><creatorcontrib>Park, In-Suk</creatorcontrib><creatorcontrib>Lee, Jeong-Ho</creatorcontrib><creatorcontrib>Lee, Sang-Jun</creatorcontrib><creatorcontrib>Kim, Kyung-Kil</creatorcontrib><title>Purification, characterization, and gene cloning of glucose-1-phosphatase from Citrobacter braakii</title><title>Journal of general and applied microbiology</title><addtitle>J. Gen. Appl. Microbiol.</addtitle><description>Citrobacter braakii produced an intracellular acid glucose phosphatase (AgpC) which was purified 986 fold to homogeneity with the specific activity of 286 units/mg. AgpC hydrolyzed a wide variety of phosphorylated compounds with high activity for glucose-1-phosphate and glucose-6-phosphate. The optimum pH and temperature for the enzyme activity was pH 5.0 and 45°C, respectively. The Km value for glucose-1-phosphate was 5.12 mM with a Vmax 27.8 U mg-1. Its molecular weight was 46 kDa by SDS-PAGE gel and the sequence of N-terminal amino acid residues identified was Gln-Thr-Ala-Pro-Glu-Gly-Tyr-Gln-Leu-Gln. The glucose-1-phosphatase gene (agpC) was cloned from the C. braakii genomic library. This gene comprised 1,242 nucleotides and encoded a polypeptide of 413 amino acids. The result of its BLAST search showed a significant similarity with glucose-1-phosphatase from enterobacteria such as E. coli, Enterobacter, Shigella, and Salmonella.</description><subject>Amino Acid Sequence</subject><subject>Citrobacter</subject><subject>Citrobacter - chemistry</subject><subject>Citrobacter - genetics</subject><subject>Citrobacter - isolation & purification</subject><subject>Citrobacter braakii</subject><subject>cloning</subject><subject>Cloning, Molecular</subject><subject>Dipeptides - analysis</subject><subject>Enterobacter</subject><subject>Escherichia coli</subject><subject>glucose-1-phosphatase</subject><subject>Glucosephosphates - analysis</subject><subject>Molecular Sequence Data</subject><subject>Peptide Fragments</subject><subject>Phylogeny</subject><subject>Protein Conformation</subject><subject>Salmonella</subject><subject>Shigella</subject><subject>substrate specificity</subject><issn>0022-1260</issn><issn>1349-8037</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp90cGL1DAUBvAgLu7s6sm7FAQ9aMeXvCZtbivDqgsLuwc9hzRNOhnbZkzag_71ZpxhBA9e8kLy44PHR8hLCmuGDD_sej2uOV9jxZ-QFcVKlg1g_ZSsABgrKRNwSa5S2gGgYE31jFxSKSvABlakfVyid97o2YfpfWG2Omoz2-h_nV701BW9nWxhhjD5qS-CK_phMSHZkpb7bUj7rZ51soWLYSw2fo6h_RNRtFHr794_JxdOD8m-OM1r8u3T7dfNl_L-4fPd5uN9abio5lJLroV1DrThTLKuOlwFthRkx0Vbd40AiiBq5NIJh62khjmsAQRvKqR4Td4ec_cx_FhsmtXok7HDoCcblqRqRJkZhSzf_FcySiUX0GT4-h-4C0uc8haKVihZUwsqsnp3VCaGlKJ1ah_9qONPRUEdKlKHihTnKleU9atT5tKOtvtrT51kcHMEuzTr3p6BjrM3gz2H8eORM89fh_qUnfA3fiyi-Q</recordid><startdate>2009</startdate><enddate>2009</enddate><creator>Kim, Young-Ok</creator><creator>Kim, Han-Woo</creator><creator>Park, In-Suk</creator><creator>Lee, Jeong-Ho</creator><creator>Lee, Sang-Jun</creator><creator>Kim, Kyung-Kil</creator><general>Applied Microbiology, Molecular and Cellular Biosciences Research Foundation</general><general>Japan Science and Technology Agency</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7T7</scope><scope>7U7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7QO</scope><scope>F1W</scope><scope>H95</scope><scope>H97</scope><scope>L.G</scope><scope>7X8</scope></search><sort><creationdate>2009</creationdate><title>Purification, characterization, and gene cloning of glucose-1-phosphatase from Citrobacter braakii</title><author>Kim, Young-Ok ; Kim, Han-Woo ; Park, In-Suk ; Lee, Jeong-Ho ; Lee, Sang-Jun ; Kim, Kyung-Kil</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c564t-a95a6eff0ac5292d4ff0a63b109d56b7d86013067359f6f3b91c2f37006584313</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Amino Acid Sequence</topic><topic>Citrobacter</topic><topic>Citrobacter - chemistry</topic><topic>Citrobacter - genetics</topic><topic>Citrobacter - isolation & purification</topic><topic>Citrobacter braakii</topic><topic>cloning</topic><topic>Cloning, Molecular</topic><topic>Dipeptides - analysis</topic><topic>Enterobacter</topic><topic>Escherichia coli</topic><topic>glucose-1-phosphatase</topic><topic>Glucosephosphates - analysis</topic><topic>Molecular Sequence Data</topic><topic>Peptide Fragments</topic><topic>Phylogeny</topic><topic>Protein Conformation</topic><topic>Salmonella</topic><topic>Shigella</topic><topic>substrate specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kim, Young-Ok</creatorcontrib><creatorcontrib>Kim, Han-Woo</creatorcontrib><creatorcontrib>Park, In-Suk</creatorcontrib><creatorcontrib>Lee, Jeong-Ho</creatorcontrib><creatorcontrib>Lee, Sang-Jun</creatorcontrib><creatorcontrib>Kim, Kyung-Kil</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Toxicology Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>Biotechnology Research Abstracts</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 3: Aquatic Pollution & Environmental Quality</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of general and applied microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kim, Young-Ok</au><au>Kim, Han-Woo</au><au>Park, In-Suk</au><au>Lee, Jeong-Ho</au><au>Lee, Sang-Jun</au><au>Kim, Kyung-Kil</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification, characterization, and gene cloning of glucose-1-phosphatase from Citrobacter braakii</atitle><jtitle>Journal of general and applied microbiology</jtitle><addtitle>J. Gen. Appl. Microbiol.</addtitle><date>2009</date><risdate>2009</risdate><volume>55</volume><issue>5</issue><spage>345</spage><epage>350</epage><pages>345-350</pages><issn>0022-1260</issn><eissn>1349-8037</eissn><abstract>Citrobacter braakii produced an intracellular acid glucose phosphatase (AgpC) which was purified 986 fold to homogeneity with the specific activity of 286 units/mg. AgpC hydrolyzed a wide variety of phosphorylated compounds with high activity for glucose-1-phosphate and glucose-6-phosphate. The optimum pH and temperature for the enzyme activity was pH 5.0 and 45°C, respectively. The Km value for glucose-1-phosphate was 5.12 mM with a Vmax 27.8 U mg-1. Its molecular weight was 46 kDa by SDS-PAGE gel and the sequence of N-terminal amino acid residues identified was Gln-Thr-Ala-Pro-Glu-Gly-Tyr-Gln-Leu-Gln. The glucose-1-phosphatase gene (agpC) was cloned from the C. braakii genomic library. 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| subjects | Amino Acid Sequence Citrobacter Citrobacter - chemistry Citrobacter - genetics Citrobacter - isolation & purification Citrobacter braakii cloning Cloning, Molecular Dipeptides - analysis Enterobacter Escherichia coli glucose-1-phosphatase Glucosephosphates - analysis Molecular Sequence Data Peptide Fragments Phylogeny Protein Conformation Salmonella Shigella substrate specificity |
| title | Purification, characterization, and gene cloning of glucose-1-phosphatase from Citrobacter braakii |
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