Effect of mutagenesis at the region upstream from the G(Q/E) motif of three types of geranylgeranyl diphosphate synthase on product chain-length
(All- E) geranylgeranyl diphosphate synthases have been classified into three types based on the characteristic sequences around the first aspartate rich motif, which is highly conserved among the enzymes. In type I geranylgeranyl diphosphate synthases, which consist of archaeal enzymes, a bulky ami...
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| creator | Noike, Motoyoshi Katagiri, Takashi Nakayama, Toru Nishino, Tokuzo Hemmi, Hisashi |
| description | (All-
E) geranylgeranyl diphosphate synthases have been classified into three types based on the characteristic sequences around the first aspartate rich motif, which is highly conserved among the enzymes. In type I geranylgeranyl diphosphate synthases, which consist of archaeal enzymes, a bulky amino acid residue at the 5th position upstream from the motif plays a main role in the product determination, by blocking further elongation of prenyl chain as the bottom of the reaction cavity. On the other hand, type III geranylgeranyl diphosphate synthases, which consist of the enzymes from eukaryotes except for plants, use a bulky amino acid residue at the 2nd position upstream from the conserved G(Q/E) motif for product chain-length determination. Thus we introduced mutations into the region upstream from the G(Q/E) motif of geranylgeranyl diphosphate synthases of the three different types to confirm the importance of the region for the product chain-length determination. The results of the mutational analyses indicated that not only the 2nd but also the 3rd position upstream from the G(Q/E) motif is involved in the product chain-length determination mechanism in types I and III geranylgeranyl diphosphate synthases, while the amino acid substitution in this region did not affect the chain-length of the products of type II geranylgeranyl diphosphate synthase, which consist of the enzymes from bacteria and plants. The region upstream from the G(Q/E) motif possibly contributes to the product determination in the wide range of geranylgeranyl diphosphate synthases, as well as that around the first aspartate rich motif. |
| doi_str_mv | 10.1016/j.jbiosc.2008.11.004 |
| format | Article |
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E) geranylgeranyl diphosphate synthases have been classified into three types based on the characteristic sequences around the first aspartate rich motif, which is highly conserved among the enzymes. In type I geranylgeranyl diphosphate synthases, which consist of archaeal enzymes, a bulky amino acid residue at the 5th position upstream from the motif plays a main role in the product determination, by blocking further elongation of prenyl chain as the bottom of the reaction cavity. On the other hand, type III geranylgeranyl diphosphate synthases, which consist of the enzymes from eukaryotes except for plants, use a bulky amino acid residue at the 2nd position upstream from the conserved G(Q/E) motif for product chain-length determination. Thus we introduced mutations into the region upstream from the G(Q/E) motif of geranylgeranyl diphosphate synthases of the three different types to confirm the importance of the region for the product chain-length determination. The results of the mutational analyses indicated that not only the 2nd but also the 3rd position upstream from the G(Q/E) motif is involved in the product chain-length determination mechanism in types I and III geranylgeranyl diphosphate synthases, while the amino acid substitution in this region did not affect the chain-length of the products of type II geranylgeranyl diphosphate synthase, which consist of the enzymes from bacteria and plants. The region upstream from the G(Q/E) motif possibly contributes to the product determination in the wide range of geranylgeranyl diphosphate synthases, as well as that around the first aspartate rich motif.</description><identifier>ISSN: 1389-1723</identifier><identifier>EISSN: 1347-4421</identifier><identifier>DOI: 10.1016/j.jbiosc.2008.11.004</identifier><identifier>PMID: 19269584</identifier><language>eng</language><publisher>Amsterdam: Elsevier B.V</publisher><subject>Amino Acid Motifs ; Amino Acid Sequence ; Archaeal Proteins - chemistry ; Archaeal Proteins - genetics ; Archaeal Proteins - metabolism ; Aspartic Acid - metabolism ; Bacterial Proteins - chemistry ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Biological and medical sciences ; BIOSINTESIS ; BIOSYNTHESE ; BIOSYNTHESIS ; Biotechnology ; ENZIMAS ; ENZYME ; ENZYMES ; Farnesyltranstransferase - chemistry ; Farnesyltranstransferase - genetics ; Farnesyltranstransferase - metabolism ; Fundamental and applied biological sciences. Psychology ; Geranylgeranyl diphosphate synthase ; Isoprenoid ; ISOPRENOIDE ; ISOPRENOIDES ; ISOPRENOIDS ; METABOLITE SECONDAIRE ; METABOLITOS SECUNDARIOS ; Molecular Sequence Data ; MUTACION ; Mutagenesis ; MUTATION ; Pantoea - enzymology ; Prenyltransferase ; Product determination ; SACCHAROMYCES CEREVISIAE ; Saccharomyces cerevisiae - enzymology ; Saccharomyces cerevisiae Proteins - chemistry ; Saccharomyces cerevisiae Proteins - genetics ; Saccharomyces cerevisiae Proteins - metabolism ; SECONDARY METABOLITES ; Sequence Homology, Amino Acid ; Sulfolobus acidocaldarius - enzymology</subject><ispartof>Journal of bioscience and bioengineering, 2009-03, Vol.107 (3), p.235-239</ispartof><rights>2008 The Society for Biotechnology, Japan</rights><rights>2009 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c535t-5e96b1508f36e3bb0213f629ea9d427f64d65ca9de556d2a5e59af3fda3a80b83</citedby><cites>FETCH-LOGICAL-c535t-5e96b1508f36e3bb0213f629ea9d427f64d65ca9de556d2a5e59af3fda3a80b83</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.jbiosc.2008.11.004$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=21348961$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19269584$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Noike, Motoyoshi</creatorcontrib><creatorcontrib>Katagiri, Takashi</creatorcontrib><creatorcontrib>Nakayama, Toru</creatorcontrib><creatorcontrib>Nishino, Tokuzo</creatorcontrib><creatorcontrib>Hemmi, Hisashi</creatorcontrib><title>Effect of mutagenesis at the region upstream from the G(Q/E) motif of three types of geranylgeranyl diphosphate synthase on product chain-length</title><title>Journal of bioscience and bioengineering</title><addtitle>J Biosci Bioeng</addtitle><description>(All-
E) geranylgeranyl diphosphate synthases have been classified into three types based on the characteristic sequences around the first aspartate rich motif, which is highly conserved among the enzymes. In type I geranylgeranyl diphosphate synthases, which consist of archaeal enzymes, a bulky amino acid residue at the 5th position upstream from the motif plays a main role in the product determination, by blocking further elongation of prenyl chain as the bottom of the reaction cavity. On the other hand, type III geranylgeranyl diphosphate synthases, which consist of the enzymes from eukaryotes except for plants, use a bulky amino acid residue at the 2nd position upstream from the conserved G(Q/E) motif for product chain-length determination. Thus we introduced mutations into the region upstream from the G(Q/E) motif of geranylgeranyl diphosphate synthases of the three different types to confirm the importance of the region for the product chain-length determination. The results of the mutational analyses indicated that not only the 2nd but also the 3rd position upstream from the G(Q/E) motif is involved in the product chain-length determination mechanism in types I and III geranylgeranyl diphosphate synthases, while the amino acid substitution in this region did not affect the chain-length of the products of type II geranylgeranyl diphosphate synthase, which consist of the enzymes from bacteria and plants. The region upstream from the G(Q/E) motif possibly contributes to the product determination in the wide range of geranylgeranyl diphosphate synthases, as well as that around the first aspartate rich motif.</description><subject>Amino Acid Motifs</subject><subject>Amino Acid Sequence</subject><subject>Archaeal Proteins - chemistry</subject><subject>Archaeal Proteins - genetics</subject><subject>Archaeal Proteins - metabolism</subject><subject>Aspartic Acid - metabolism</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Biological and medical sciences</subject><subject>BIOSINTESIS</subject><subject>BIOSYNTHESE</subject><subject>BIOSYNTHESIS</subject><subject>Biotechnology</subject><subject>ENZIMAS</subject><subject>ENZYME</subject><subject>ENZYMES</subject><subject>Farnesyltranstransferase - chemistry</subject><subject>Farnesyltranstransferase - genetics</subject><subject>Farnesyltranstransferase - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Geranylgeranyl diphosphate synthase</subject><subject>Isoprenoid</subject><subject>ISOPRENOIDE</subject><subject>ISOPRENOIDES</subject><subject>ISOPRENOIDS</subject><subject>METABOLITE SECONDAIRE</subject><subject>METABOLITOS SECUNDARIOS</subject><subject>Molecular Sequence Data</subject><subject>MUTACION</subject><subject>Mutagenesis</subject><subject>MUTATION</subject><subject>Pantoea - enzymology</subject><subject>Prenyltransferase</subject><subject>Product determination</subject><subject>SACCHAROMYCES CEREVISIAE</subject><subject>Saccharomyces cerevisiae - enzymology</subject><subject>Saccharomyces cerevisiae Proteins - chemistry</subject><subject>Saccharomyces cerevisiae Proteins - genetics</subject><subject>Saccharomyces cerevisiae Proteins - metabolism</subject><subject>SECONDARY METABOLITES</subject><subject>Sequence Homology, Amino Acid</subject><subject>Sulfolobus acidocaldarius - enzymology</subject><issn>1389-1723</issn><issn>1347-4421</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kU2L1TAUhosozjj6D1SyUXTRTtJ8tN0IMlxHZUAFXYc0PbnNpW06SSrcf-FPNrVFd65ODuc5H3nfLHtOcEEwEden4tRaF3RRYlwXhBQYswfZJaGsyhkrycP1XTc5qUp6kT0J4YQxqXBFHmcXpClFw2t2mf06GAM6ImfQuER1hAmCDUhFFHtAHo7WTWiZQ_SgRmS8G_8Ubt98uz68RaOL1qy9sfcAKJ5nCGt6BK-m87AH1Nm5d2HuVQQUzlPsVQCU5s7edUtarntlp3yA6Rj7p9kjo4YAz_Z4lf34cPh-8zG_-3L76eb9Xa455THn0IiWcFwbKoC2LS4JNaJsQDUdKysjWCe4TglwLrpSceCNMtR0iqoatzW9yl5vc9MR9wuEKEcbNAyDmsAtQZaYVUlLkkC2gdq7EDwYOXs7Kn-WBMvVCXmSmxNydUISIpMTqe3lPn9pR-j-Ne3SJ-DVDqig1WCSVNqGv1z6D6sbse5_sXFGOamOPjGfv6ZNDca0EiLV3211SGr9tOBl0BYmDZ31yVnZOfv_S38DP5uz6A</recordid><startdate>20090301</startdate><enddate>20090301</enddate><creator>Noike, Motoyoshi</creator><creator>Katagiri, Takashi</creator><creator>Nakayama, Toru</creator><creator>Nishino, Tokuzo</creator><creator>Hemmi, Hisashi</creator><general>Elsevier B.V</general><general>Elsevier</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>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7QO</scope><scope>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope></search><sort><creationdate>20090301</creationdate><title>Effect of mutagenesis at the region upstream from the G(Q/E) motif of three types of geranylgeranyl diphosphate synthase on product chain-length</title><author>Noike, Motoyoshi ; Katagiri, Takashi ; Nakayama, Toru ; Nishino, Tokuzo ; Hemmi, Hisashi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c535t-5e96b1508f36e3bb0213f629ea9d427f64d65ca9de556d2a5e59af3fda3a80b83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Amino Acid Motifs</topic><topic>Amino Acid Sequence</topic><topic>Archaeal Proteins - chemistry</topic><topic>Archaeal Proteins - genetics</topic><topic>Archaeal Proteins - metabolism</topic><topic>Aspartic Acid - metabolism</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - metabolism</topic><topic>Biological and medical sciences</topic><topic>BIOSINTESIS</topic><topic>BIOSYNTHESE</topic><topic>BIOSYNTHESIS</topic><topic>Biotechnology</topic><topic>ENZIMAS</topic><topic>ENZYME</topic><topic>ENZYMES</topic><topic>Farnesyltranstransferase - chemistry</topic><topic>Farnesyltranstransferase - genetics</topic><topic>Farnesyltranstransferase - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Geranylgeranyl diphosphate synthase</topic><topic>Isoprenoid</topic><topic>ISOPRENOIDE</topic><topic>ISOPRENOIDES</topic><topic>ISOPRENOIDS</topic><topic>METABOLITE SECONDAIRE</topic><topic>METABOLITOS SECUNDARIOS</topic><topic>Molecular Sequence Data</topic><topic>MUTACION</topic><topic>Mutagenesis</topic><topic>MUTATION</topic><topic>Pantoea - enzymology</topic><topic>Prenyltransferase</topic><topic>Product determination</topic><topic>SACCHAROMYCES CEREVISIAE</topic><topic>Saccharomyces cerevisiae - enzymology</topic><topic>Saccharomyces cerevisiae Proteins - chemistry</topic><topic>Saccharomyces cerevisiae Proteins - genetics</topic><topic>Saccharomyces cerevisiae Proteins - metabolism</topic><topic>SECONDARY METABOLITES</topic><topic>Sequence Homology, Amino Acid</topic><topic>Sulfolobus acidocaldarius - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Noike, Motoyoshi</creatorcontrib><creatorcontrib>Katagiri, Takashi</creatorcontrib><creatorcontrib>Nakayama, Toru</creatorcontrib><creatorcontrib>Nishino, Tokuzo</creatorcontrib><creatorcontrib>Hemmi, Hisashi</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>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Journal of bioscience and bioengineering</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Noike, Motoyoshi</au><au>Katagiri, Takashi</au><au>Nakayama, Toru</au><au>Nishino, Tokuzo</au><au>Hemmi, Hisashi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Effect of mutagenesis at the region upstream from the G(Q/E) motif of three types of geranylgeranyl diphosphate synthase on product chain-length</atitle><jtitle>Journal of bioscience and bioengineering</jtitle><addtitle>J Biosci Bioeng</addtitle><date>2009-03-01</date><risdate>2009</risdate><volume>107</volume><issue>3</issue><spage>235</spage><epage>239</epage><pages>235-239</pages><issn>1389-1723</issn><eissn>1347-4421</eissn><abstract>(All-
E) geranylgeranyl diphosphate synthases have been classified into three types based on the characteristic sequences around the first aspartate rich motif, which is highly conserved among the enzymes. In type I geranylgeranyl diphosphate synthases, which consist of archaeal enzymes, a bulky amino acid residue at the 5th position upstream from the motif plays a main role in the product determination, by blocking further elongation of prenyl chain as the bottom of the reaction cavity. On the other hand, type III geranylgeranyl diphosphate synthases, which consist of the enzymes from eukaryotes except for plants, use a bulky amino acid residue at the 2nd position upstream from the conserved G(Q/E) motif for product chain-length determination. Thus we introduced mutations into the region upstream from the G(Q/E) motif of geranylgeranyl diphosphate synthases of the three different types to confirm the importance of the region for the product chain-length determination. The results of the mutational analyses indicated that not only the 2nd but also the 3rd position upstream from the G(Q/E) motif is involved in the product chain-length determination mechanism in types I and III geranylgeranyl diphosphate synthases, while the amino acid substitution in this region did not affect the chain-length of the products of type II geranylgeranyl diphosphate synthase, which consist of the enzymes from bacteria and plants. The region upstream from the G(Q/E) motif possibly contributes to the product determination in the wide range of geranylgeranyl diphosphate synthases, as well as that around the first aspartate rich motif.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><pmid>19269584</pmid><doi>10.1016/j.jbiosc.2008.11.004</doi><tpages>5</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1389-1723 |
| ispartof | Journal of bioscience and bioengineering, 2009-03, Vol.107 (3), p.235-239 |
| issn | 1389-1723 1347-4421 |
| language | eng |
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| source | MEDLINE; Access via ScienceDirect (Elsevier) |
| subjects | Amino Acid Motifs Amino Acid Sequence Archaeal Proteins - chemistry Archaeal Proteins - genetics Archaeal Proteins - metabolism Aspartic Acid - metabolism Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Biological and medical sciences BIOSINTESIS BIOSYNTHESE BIOSYNTHESIS Biotechnology ENZIMAS ENZYME ENZYMES Farnesyltranstransferase - chemistry Farnesyltranstransferase - genetics Farnesyltranstransferase - metabolism Fundamental and applied biological sciences. Psychology Geranylgeranyl diphosphate synthase Isoprenoid ISOPRENOIDE ISOPRENOIDES ISOPRENOIDS METABOLITE SECONDAIRE METABOLITOS SECUNDARIOS Molecular Sequence Data MUTACION Mutagenesis MUTATION Pantoea - enzymology Prenyltransferase Product determination SACCHAROMYCES CEREVISIAE Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism SECONDARY METABOLITES Sequence Homology, Amino Acid Sulfolobus acidocaldarius - enzymology |
| title | Effect of mutagenesis at the region upstream from the G(Q/E) motif of three types of geranylgeranyl diphosphate synthase on product chain-length |
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