Characterization of a F280N variant of L-arabinose isomerase from Geobacillus thermodenitrificans identified as a D-galactose isomerase
The double-site variant (C450S-N475K) L-arabinose isomerase (L-AI) from Geobacillus thermodenitrificans catalyzes the isomerization of D-galactose to D-tagatose, a functional sweetener. Using a substrate-docking homology model, the residues near to D-galactose O6 were identified as Met186, Phe280, a...
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| Veröffentlicht in: | Applied microbiology and biotechnology 2014-11, Vol.98 (22), p.9271-9281 |
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| creator | Kim, Baek-Joong Hong, Seung-Hye Shin, Kyung-Chul Jo, Ye-Seul Oh, Deok-Kun |
| description | The double-site variant (C450S-N475K) L-arabinose isomerase (L-AI) from Geobacillus thermodenitrificans catalyzes the isomerization of D-galactose to D-tagatose, a functional sweetener. Using a substrate-docking homology model, the residues near to D-galactose O6 were identified as Met186, Phe280, and Ile371. Several variants obtained by site-directed mutagenesis of these three residues were analyzed, and a triple-site (F280N) variant enzyme exhibited the highest activity for D-galactose isomerization. The k cₐₜ/K ₘ of the triple-site variant enzyme for D-galactose was 2.1-fold higher than for L-arabinose, whereas the k cₐₜ/K ₘ of the double-site variant enzyme for L-arabinose was 43.9-fold higher than for D-galactose. These results suggest that the triple-site variant enzyme is a D-galactose isomerase. The conversion rate of D-galactose to D-tagatose by the triple-site variant enzyme was approximately 3-fold higher than that of the double-site variant enzyme for 30 min. However, the conversion yields of L-arabinose to L-ribulose by the triple-site and double-site variant enzymes were 10.6 and 16.0 % after 20 min, respectively. The triple-site variant enzyme exhibited increased specific activity, turnover number, catalytic efficiency, and conversion rate for D-galactose isomerization compared to the double-site variant enzyme. Therefore, the amino acid at position 280 determines the substrate specificity for D-galactose and L-arabinose, and the triple-site variant enzyme has the potential to produce D-tagatose on an industrial scale. |
| doi_str_mv | 10.1007/s00253-014-5827-z |
| format | Article |
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Using a substrate-docking homology model, the residues near to D-galactose O6 were identified as Met186, Phe280, and Ile371. Several variants obtained by site-directed mutagenesis of these three residues were analyzed, and a triple-site (F280N) variant enzyme exhibited the highest activity for D-galactose isomerization. The k cₐₜ/K ₘ of the triple-site variant enzyme for D-galactose was 2.1-fold higher than for L-arabinose, whereas the k cₐₜ/K ₘ of the double-site variant enzyme for L-arabinose was 43.9-fold higher than for D-galactose. These results suggest that the triple-site variant enzyme is a D-galactose isomerase. The conversion rate of D-galactose to D-tagatose by the triple-site variant enzyme was approximately 3-fold higher than that of the double-site variant enzyme for 30 min. However, the conversion yields of L-arabinose to L-ribulose by the triple-site and double-site variant enzymes were 10.6 and 16.0 % after 20 min, respectively. The triple-site variant enzyme exhibited increased specific activity, turnover number, catalytic efficiency, and conversion rate for D-galactose isomerization compared to the double-site variant enzyme. Therefore, the amino acid at position 280 determines the substrate specificity for D-galactose and L-arabinose, and the triple-site variant enzyme has the potential to produce D-tagatose on an industrial scale.</description><identifier>ISSN: 0175-7598</identifier><identifier>EISSN: 1432-0614</identifier><identifier>DOI: 10.1007/s00253-014-5827-z</identifier><identifier>PMID: 24880627</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer-Verlag</publisher><subject>Aldose-Ketose Isomerases - genetics ; Aldose-Ketose Isomerases - metabolism ; Amino Acid Substitution ; Amino acids ; Arabinose - metabolism ; Bacillus thermodenitrificans ; Biomedical and Life Sciences ; Biotechnologically Relevant Enzymes and Proteins ; Biotechnology ; catalytic activity ; Cloning ; Crystal structure ; E coli ; Energy ; Enzymes ; Galactose - metabolism ; Geobacillus ; Geobacillus - enzymology ; Geobacillus - genetics ; Gram-positive bacteria ; Hexoses - metabolism ; Isomerases ; isomerization ; Kinetics ; Life Sciences ; Microbial Genetics and Genomics ; Microbiology ; Mutagenesis ; Mutagenesis, Site-Directed ; Mutant Proteins - genetics ; Mutant Proteins - metabolism ; Mutation ; Mutation, Missense ; Physiological aspects ; Properties ; Proteins ; site-directed mutagenesis ; Studies ; Substrate Specificity</subject><ispartof>Applied microbiology and biotechnology, 2014-11, Vol.98 (22), p.9271-9281</ispartof><rights>Springer-Verlag Berlin Heidelberg 2014</rights><rights>COPYRIGHT 2014 Springer</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c637t-278b3320f8ce1ee7f20201850928679499c1bf30ddfcbc755edd557ec85a4b6a3</citedby><cites>FETCH-LOGICAL-c637t-278b3320f8ce1ee7f20201850928679499c1bf30ddfcbc755edd557ec85a4b6a3</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/s00253-014-5827-z$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00253-014-5827-z$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24880627$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kim, Baek-Joong</creatorcontrib><creatorcontrib>Hong, Seung-Hye</creatorcontrib><creatorcontrib>Shin, Kyung-Chul</creatorcontrib><creatorcontrib>Jo, Ye-Seul</creatorcontrib><creatorcontrib>Oh, Deok-Kun</creatorcontrib><title>Characterization of a F280N variant of L-arabinose isomerase from Geobacillus thermodenitrificans identified as a D-galactose isomerase</title><title>Applied microbiology and biotechnology</title><addtitle>Appl Microbiol Biotechnol</addtitle><addtitle>Appl Microbiol Biotechnol</addtitle><description>The double-site variant (C450S-N475K) L-arabinose isomerase (L-AI) from Geobacillus thermodenitrificans catalyzes the isomerization of D-galactose to D-tagatose, a functional sweetener. Using a substrate-docking homology model, the residues near to D-galactose O6 were identified as Met186, Phe280, and Ile371. Several variants obtained by site-directed mutagenesis of these three residues were analyzed, and a triple-site (F280N) variant enzyme exhibited the highest activity for D-galactose isomerization. The k cₐₜ/K ₘ of the triple-site variant enzyme for D-galactose was 2.1-fold higher than for L-arabinose, whereas the k cₐₜ/K ₘ of the double-site variant enzyme for L-arabinose was 43.9-fold higher than for D-galactose. These results suggest that the triple-site variant enzyme is a D-galactose isomerase. The conversion rate of D-galactose to D-tagatose by the triple-site variant enzyme was approximately 3-fold higher than that of the double-site variant enzyme for 30 min. However, the conversion yields of L-arabinose to L-ribulose by the triple-site and double-site variant enzymes were 10.6 and 16.0 % after 20 min, respectively. The triple-site variant enzyme exhibited increased specific activity, turnover number, catalytic efficiency, and conversion rate for D-galactose isomerization compared to the double-site variant enzyme. Therefore, the amino acid at position 280 determines the substrate specificity for D-galactose and L-arabinose, and the triple-site variant enzyme has the potential to produce D-tagatose on an industrial scale.</description><subject>Aldose-Ketose Isomerases - genetics</subject><subject>Aldose-Ketose Isomerases - metabolism</subject><subject>Amino Acid Substitution</subject><subject>Amino acids</subject><subject>Arabinose - metabolism</subject><subject>Bacillus thermodenitrificans</subject><subject>Biomedical and Life Sciences</subject><subject>Biotechnologically Relevant Enzymes and Proteins</subject><subject>Biotechnology</subject><subject>catalytic activity</subject><subject>Cloning</subject><subject>Crystal structure</subject><subject>E coli</subject><subject>Energy</subject><subject>Enzymes</subject><subject>Galactose - metabolism</subject><subject>Geobacillus</subject><subject>Geobacillus - enzymology</subject><subject>Geobacillus - genetics</subject><subject>Gram-positive bacteria</subject><subject>Hexoses - metabolism</subject><subject>Isomerases</subject><subject>isomerization</subject><subject>Kinetics</subject><subject>Life Sciences</subject><subject>Microbial Genetics and Genomics</subject><subject>Microbiology</subject><subject>Mutagenesis</subject><subject>Mutagenesis, Site-Directed</subject><subject>Mutant Proteins - genetics</subject><subject>Mutant Proteins - metabolism</subject><subject>Mutation</subject><subject>Mutation, Missense</subject><subject>Physiological aspects</subject><subject>Properties</subject><subject>Proteins</subject><subject>site-directed mutagenesis</subject><subject>Studies</subject><subject>Substrate 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of a F280N variant of L-arabinose isomerase from Geobacillus thermodenitrificans identified as a D-galactose isomerase</title><author>Kim, Baek-Joong ; Hong, Seung-Hye ; Shin, Kyung-Chul ; Jo, Ye-Seul ; Oh, Deok-Kun</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c637t-278b3320f8ce1ee7f20201850928679499c1bf30ddfcbc755edd557ec85a4b6a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Aldose-Ketose Isomerases - genetics</topic><topic>Aldose-Ketose Isomerases - metabolism</topic><topic>Amino Acid Substitution</topic><topic>Amino acids</topic><topic>Arabinose - metabolism</topic><topic>Bacillus thermodenitrificans</topic><topic>Biomedical and Life Sciences</topic><topic>Biotechnologically Relevant Enzymes and Proteins</topic><topic>Biotechnology</topic><topic>catalytic activity</topic><topic>Cloning</topic><topic>Crystal structure</topic><topic>E coli</topic><topic>Energy</topic><topic>Enzymes</topic><topic>Galactose - metabolism</topic><topic>Geobacillus</topic><topic>Geobacillus - enzymology</topic><topic>Geobacillus - genetics</topic><topic>Gram-positive bacteria</topic><topic>Hexoses - metabolism</topic><topic>Isomerases</topic><topic>isomerization</topic><topic>Kinetics</topic><topic>Life Sciences</topic><topic>Microbial Genetics and Genomics</topic><topic>Microbiology</topic><topic>Mutagenesis</topic><topic>Mutagenesis, Site-Directed</topic><topic>Mutant Proteins - genetics</topic><topic>Mutant Proteins - metabolism</topic><topic>Mutation</topic><topic>Mutation, Missense</topic><topic>Physiological aspects</topic><topic>Properties</topic><topic>Proteins</topic><topic>site-directed mutagenesis</topic><topic>Studies</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kim, Baek-Joong</creatorcontrib><creatorcontrib>Hong, 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(Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Business</collection><collection>ProQuest One Business (Alumni)</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>Biotechnology Research Abstracts</collection><jtitle>Applied microbiology and biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kim, Baek-Joong</au><au>Hong, Seung-Hye</au><au>Shin, Kyung-Chul</au><au>Jo, Ye-Seul</au><au>Oh, Deok-Kun</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of a F280N variant of L-arabinose isomerase from Geobacillus thermodenitrificans identified as a D-galactose isomerase</atitle><jtitle>Applied microbiology and biotechnology</jtitle><stitle>Appl Microbiol Biotechnol</stitle><addtitle>Appl Microbiol Biotechnol</addtitle><date>2014-11-01</date><risdate>2014</risdate><volume>98</volume><issue>22</issue><spage>9271</spage><epage>9281</epage><pages>9271-9281</pages><issn>0175-7598</issn><eissn>1432-0614</eissn><abstract>The double-site variant (C450S-N475K) L-arabinose isomerase (L-AI) from Geobacillus thermodenitrificans catalyzes the isomerization of D-galactose to D-tagatose, a functional sweetener. Using a substrate-docking homology model, the residues near to D-galactose O6 were identified as Met186, Phe280, and Ile371. Several variants obtained by site-directed mutagenesis of these three residues were analyzed, and a triple-site (F280N) variant enzyme exhibited the highest activity for D-galactose isomerization. The k cₐₜ/K ₘ of the triple-site variant enzyme for D-galactose was 2.1-fold higher than for L-arabinose, whereas the k cₐₜ/K ₘ of the double-site variant enzyme for L-arabinose was 43.9-fold higher than for D-galactose. These results suggest that the triple-site variant enzyme is a D-galactose isomerase. The conversion rate of D-galactose to D-tagatose by the triple-site variant enzyme was approximately 3-fold higher than that of the double-site variant enzyme for 30 min. However, the conversion yields of L-arabinose to L-ribulose by the triple-site and double-site variant enzymes were 10.6 and 16.0 % after 20 min, respectively. The triple-site variant enzyme exhibited increased specific activity, turnover number, catalytic efficiency, and conversion rate for D-galactose isomerization compared to the double-site variant enzyme. Therefore, the amino acid at position 280 determines the substrate specificity for D-galactose and L-arabinose, and the triple-site variant enzyme has the potential to produce D-tagatose on an industrial scale.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer-Verlag</pub><pmid>24880627</pmid><doi>10.1007/s00253-014-5827-z</doi><tpages>11</tpages></addata></record> |
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| subjects | Aldose-Ketose Isomerases - genetics Aldose-Ketose Isomerases - metabolism Amino Acid Substitution Amino acids Arabinose - metabolism Bacillus thermodenitrificans Biomedical and Life Sciences Biotechnologically Relevant Enzymes and Proteins Biotechnology catalytic activity Cloning Crystal structure E coli Energy Enzymes Galactose - metabolism Geobacillus Geobacillus - enzymology Geobacillus - genetics Gram-positive bacteria Hexoses - metabolism Isomerases isomerization Kinetics Life Sciences Microbial Genetics and Genomics Microbiology Mutagenesis Mutagenesis, Site-Directed Mutant Proteins - genetics Mutant Proteins - metabolism Mutation Mutation, Missense Physiological aspects Properties Proteins site-directed mutagenesis Studies Substrate Specificity |
| title | Characterization of a F280N variant of L-arabinose isomerase from Geobacillus thermodenitrificans identified as a D-galactose isomerase |
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