Substrate specificity engineering of Escherichia coli derived fructosamine 6-kinase
A three-dimensional structural model of Escherichia coli fructosamine 6-kinase (FN6K), an enzyme that phosphorylates fructosamines at C6 and catalyzes the production of the fructosamine 6-phosphate stable intermediate, was generated using the crystal structure of 2-keto-3-deoxygluconate kinase isola...
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| Veröffentlicht in: | Biotechnology letters 2013-02, Vol.35 (2), p.253-258 |
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| creator | Kojima, Katsuhiro Mikami-Sakaguchi, Akane Kameya, Miho Miyamoto, Yusuke Ferri, Stefano Tsugawa, Wakako Sode, Koji |
| description | A three-dimensional structural model of Escherichia coli fructosamine 6-kinase (FN6K), an enzyme that phosphorylates fructosamines at C6 and catalyzes the production of the fructosamine 6-phosphate stable intermediate, was generated using the crystal structure of 2-keto-3-deoxygluconate kinase isolated from Thermus thermophilus as template. The putative active site region was then investigated by site-directed mutagenesis to reveal several amino acid residues that likely play important roles in the enzyme reaction. Met220 was identified as a residue that plays a role in substrate recognition when compared to Bacillus subtilis derived FN6K, which shows different substrate specificity from the E. coli FN6K. Among the various Met220-substituted mutant enzymes, Met220Leu, which corresponded to the B. subtilis residue, resulted in an increased activity of fructosyl-valine and decreased activity of fructosyl-lysine, thus increasing the specificity for fructosyl-valine by 40-fold. |
| doi_str_mv | 10.1007/s10529-012-1062-9 |
| format | Article |
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The putative active site region was then investigated by site-directed mutagenesis to reveal several amino acid residues that likely play important roles in the enzyme reaction. Met220 was identified as a residue that plays a role in substrate recognition when compared to Bacillus subtilis derived FN6K, which shows different substrate specificity from the E. coli FN6K. Among the various Met220-substituted mutant enzymes, Met220Leu, which corresponded to the B. subtilis residue, resulted in an increased activity of fructosyl-valine and decreased activity of fructosyl-lysine, thus increasing the specificity for fructosyl-valine by 40-fold.</description><identifier>ISSN: 0141-5492</identifier><identifier>EISSN: 1573-6776</identifier><identifier>DOI: 10.1007/s10529-012-1062-9</identifier><identifier>PMID: 23076362</identifier><language>eng</language><publisher>Dordrecht: Springer-Verlag</publisher><subject>Amino Acid Substitution ; Amino acids ; Applied Microbiology ; Bacillus subtilis ; Biochemistry ; Biomedical and Life Sciences ; Biotechnology ; Catalytic Domain ; Crystal structure ; E coli ; engineering ; Enzymes ; Escherichia coli ; Escherichia coli - enzymology ; Fructosamine - metabolism ; Kinases ; Life Sciences ; Lysine - analogs & derivatives ; Lysine - metabolism ; Metabolic Engineering ; Microbiology ; Models, Molecular ; Mutagenesis ; Mutagenesis, Site-Directed ; Mutant Proteins - genetics ; Mutant Proteins - metabolism ; mutants ; Original Research Paper ; Phosphotransferases - genetics ; Phosphotransferases - metabolism ; Protein Engineering ; Residues ; site-directed mutagenesis ; Substrate Specificity ; Substrates ; Thermus thermophilus ; Three dimensional models ; Valine - analogs & derivatives ; Valine - metabolism</subject><ispartof>Biotechnology letters, 2013-02, Vol.35 (2), p.253-258</ispartof><rights>Springer Science+Business Media Dordrecht 2012</rights><rights>Springer Science+Business Media Dordrecht 2013</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c552t-95d796e9183986444200de2c12c49cdbc4b7a946849b74d02b4b856f2b6afe63</citedby><cites>FETCH-LOGICAL-c552t-95d796e9183986444200de2c12c49cdbc4b7a946849b74d02b4b856f2b6afe63</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s10529-012-1062-9$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s10529-012-1062-9$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>315,781,785,27929,27930,41493,42562,51324</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23076362$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kojima, Katsuhiro</creatorcontrib><creatorcontrib>Mikami-Sakaguchi, Akane</creatorcontrib><creatorcontrib>Kameya, Miho</creatorcontrib><creatorcontrib>Miyamoto, Yusuke</creatorcontrib><creatorcontrib>Ferri, Stefano</creatorcontrib><creatorcontrib>Tsugawa, Wakako</creatorcontrib><creatorcontrib>Sode, Koji</creatorcontrib><title>Substrate specificity engineering of Escherichia coli derived fructosamine 6-kinase</title><title>Biotechnology letters</title><addtitle>Biotechnol Lett</addtitle><addtitle>Biotechnol Lett</addtitle><description>A three-dimensional structural model of Escherichia coli fructosamine 6-kinase (FN6K), an enzyme that phosphorylates fructosamines at C6 and catalyzes the production of the fructosamine 6-phosphate stable intermediate, was generated using the crystal structure of 2-keto-3-deoxygluconate kinase isolated from Thermus thermophilus as template. The putative active site region was then investigated by site-directed mutagenesis to reveal several amino acid residues that likely play important roles in the enzyme reaction. Met220 was identified as a residue that plays a role in substrate recognition when compared to Bacillus subtilis derived FN6K, which shows different substrate specificity from the E. coli FN6K. Among the various Met220-substituted mutant enzymes, Met220Leu, which corresponded to the B. subtilis residue, resulted in an increased activity of fructosyl-valine and decreased activity of fructosyl-lysine, thus increasing the specificity for fructosyl-valine by 40-fold.</description><subject>Amino Acid Substitution</subject><subject>Amino acids</subject><subject>Applied Microbiology</subject><subject>Bacillus subtilis</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Biotechnology</subject><subject>Catalytic Domain</subject><subject>Crystal structure</subject><subject>E coli</subject><subject>engineering</subject><subject>Enzymes</subject><subject>Escherichia coli</subject><subject>Escherichia coli - enzymology</subject><subject>Fructosamine - metabolism</subject><subject>Kinases</subject><subject>Life Sciences</subject><subject>Lysine - analogs & derivatives</subject><subject>Lysine - metabolism</subject><subject>Metabolic Engineering</subject><subject>Microbiology</subject><subject>Models, Molecular</subject><subject>Mutagenesis</subject><subject>Mutagenesis, Site-Directed</subject><subject>Mutant Proteins - genetics</subject><subject>Mutant Proteins - metabolism</subject><subject>mutants</subject><subject>Original Research Paper</subject><subject>Phosphotransferases - genetics</subject><subject>Phosphotransferases - metabolism</subject><subject>Protein Engineering</subject><subject>Residues</subject><subject>site-directed mutagenesis</subject><subject>Substrate Specificity</subject><subject>Substrates</subject><subject>Thermus thermophilus</subject><subject>Three dimensional models</subject><subject>Valine - analogs & derivatives</subject><subject>Valine - 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The putative active site region was then investigated by site-directed mutagenesis to reveal several amino acid residues that likely play important roles in the enzyme reaction. Met220 was identified as a residue that plays a role in substrate recognition when compared to Bacillus subtilis derived FN6K, which shows different substrate specificity from the E. coli FN6K. Among the various Met220-substituted mutant enzymes, Met220Leu, which corresponded to the B. subtilis residue, resulted in an increased activity of fructosyl-valine and decreased activity of fructosyl-lysine, thus increasing the specificity for fructosyl-valine by 40-fold.</abstract><cop>Dordrecht</cop><pub>Springer-Verlag</pub><pmid>23076362</pmid><doi>10.1007/s10529-012-1062-9</doi><tpages>6</tpages></addata></record> |
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| subjects | Amino Acid Substitution Amino acids Applied Microbiology Bacillus subtilis Biochemistry Biomedical and Life Sciences Biotechnology Catalytic Domain Crystal structure E coli engineering Enzymes Escherichia coli Escherichia coli - enzymology Fructosamine - metabolism Kinases Life Sciences Lysine - analogs & derivatives Lysine - metabolism Metabolic Engineering Microbiology Models, Molecular Mutagenesis Mutagenesis, Site-Directed Mutant Proteins - genetics Mutant Proteins - metabolism mutants Original Research Paper Phosphotransferases - genetics Phosphotransferases - metabolism Protein Engineering Residues site-directed mutagenesis Substrate Specificity Substrates Thermus thermophilus Three dimensional models Valine - analogs & derivatives Valine - metabolism |
| title | Substrate specificity engineering of Escherichia coli derived fructosamine 6-kinase |
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