Akihide Yoshihara*, Erika Miyoshi, Shunsuke Tomino, Yusuke Hanaki, Susumu Mochizuki, Hiromi Yoshida, Ken Izumori and Shigehiro Kamitori*,
{"title":"转醛醇酶合成8碳和9碳糖的研究。","authors":"Akihide Yoshihara*, Erika Miyoshi, Shunsuke Tomino, Yusuke Hanaki, Susumu Mochizuki, Hiromi Yoshida, Ken Izumori and Shigehiro Kamitori*, ","doi":"10.1021/acs.jafc.5c05539","DOIUrl":null,"url":null,"abstract":"<p >In nature, higher carbon sugars composed of 7 or more carbons exist in limited quantities. Since some higher carbon sugars have attracted attention due to their biological activities, it is necessary to develop a strategy to synthesize them. Transaldolase catalyzes the transfer of three-carbon units from <span>d</span>-fructose-6-phosphate (donor) to <span>d</span>-erythrulose-4-phosphate (acceptor) to produce <span>d</span>-sedoheptulose-7-phosphate. If transaldolase can recognize nonphosphorylated monosaccharides as substrates, it can synthesize 8-carbon octuloses and 9-carbon nonuloses using nonphosphorylated pentoses and hexoses as acceptors, respectively. We performed biochemical and structural characterization of thermophilic <i>Thermus thermophilus</i> HB8 transaldolase and successfully synthesized octuloses and nonuloses using nonphosphorylated aldoses as acceptors: <span>d</span>-ribose (conversion rate of 74%), <span>d</span>-xylose (55%), <span>l</span>-arabinose (49%), <span>l</span>-lyxose (84%), <span>d</span>-allose (13%), <span>d</span>-galactose (56%), and <span>l</span>-altrose (71%). Products were identified by LC/MS and NMR spectroscopic analyses. X-ray structure of the enzyme showed that the wide and hydrophilic catalytic site facilitates the binding of nonphosphorylated aldoses as acceptors.</p>","PeriodicalId":41,"journal":{"name":"Journal of Agricultural and Food Chemistry","volume":"73 30","pages":"18914–18922"},"PeriodicalIF":6.2000,"publicationDate":"2025-07-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Synthetic Study of 8- and 9-Carbon Sugars by Transaldolase\",\"authors\":\"Akihide Yoshihara*, Erika Miyoshi, Shunsuke Tomino, Yusuke Hanaki, Susumu Mochizuki, Hiromi Yoshida, Ken Izumori and Shigehiro Kamitori*, \",\"doi\":\"10.1021/acs.jafc.5c05539\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p >In nature, higher carbon sugars composed of 7 or more carbons exist in limited quantities. Since some higher carbon sugars have attracted attention due to their biological activities, it is necessary to develop a strategy to synthesize them. Transaldolase catalyzes the transfer of three-carbon units from <span>d</span>-fructose-6-phosphate (donor) to <span>d</span>-erythrulose-4-phosphate (acceptor) to produce <span>d</span>-sedoheptulose-7-phosphate. If transaldolase can recognize nonphosphorylated monosaccharides as substrates, it can synthesize 8-carbon octuloses and 9-carbon nonuloses using nonphosphorylated pentoses and hexoses as acceptors, respectively. We performed biochemical and structural characterization of thermophilic <i>Thermus thermophilus</i> HB8 transaldolase and successfully synthesized octuloses and nonuloses using nonphosphorylated aldoses as acceptors: <span>d</span>-ribose (conversion rate of 74%), <span>d</span>-xylose (55%), <span>l</span>-arabinose (49%), <span>l</span>-lyxose (84%), <span>d</span>-allose (13%), <span>d</span>-galactose (56%), and <span>l</span>-altrose (71%). Products were identified by LC/MS and NMR spectroscopic analyses. X-ray structure of the enzyme showed that the wide and hydrophilic catalytic site facilitates the binding of nonphosphorylated aldoses as acceptors.</p>\",\"PeriodicalId\":41,\"journal\":{\"name\":\"Journal of Agricultural and Food Chemistry\",\"volume\":\"73 30\",\"pages\":\"18914–18922\"},\"PeriodicalIF\":6.2000,\"publicationDate\":\"2025-07-16\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of Agricultural and Food Chemistry\",\"FirstCategoryId\":\"97\",\"ListUrlMain\":\"https://pubs.acs.org/doi/10.1021/acs.jafc.5c05539\",\"RegionNum\":1,\"RegionCategory\":\"农林科学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"AGRICULTURE, MULTIDISCIPLINARY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Agricultural and Food Chemistry","FirstCategoryId":"97","ListUrlMain":"https://pubs.acs.org/doi/10.1021/acs.jafc.5c05539","RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"AGRICULTURE, MULTIDISCIPLINARY","Score":null,"Total":0}
Synthetic Study of 8- and 9-Carbon Sugars by Transaldolase
In nature, higher carbon sugars composed of 7 or more carbons exist in limited quantities. Since some higher carbon sugars have attracted attention due to their biological activities, it is necessary to develop a strategy to synthesize them. Transaldolase catalyzes the transfer of three-carbon units from d-fructose-6-phosphate (donor) to d-erythrulose-4-phosphate (acceptor) to produce d-sedoheptulose-7-phosphate. If transaldolase can recognize nonphosphorylated monosaccharides as substrates, it can synthesize 8-carbon octuloses and 9-carbon nonuloses using nonphosphorylated pentoses and hexoses as acceptors, respectively. We performed biochemical and structural characterization of thermophilic Thermus thermophilus HB8 transaldolase and successfully synthesized octuloses and nonuloses using nonphosphorylated aldoses as acceptors: d-ribose (conversion rate of 74%), d-xylose (55%), l-arabinose (49%), l-lyxose (84%), d-allose (13%), d-galactose (56%), and l-altrose (71%). Products were identified by LC/MS and NMR spectroscopic analyses. X-ray structure of the enzyme showed that the wide and hydrophilic catalytic site facilitates the binding of nonphosphorylated aldoses as acceptors.
期刊介绍:
The Journal of Agricultural and Food Chemistry publishes high-quality, cutting edge original research representing complete studies and research advances dealing with the chemistry and biochemistry of agriculture and food. The Journal also encourages papers with chemistry and/or biochemistry as a major component combined with biological/sensory/nutritional/toxicological evaluation related to agriculture and/or food.