The LPG1x family from Leishmania major is constituted of rare eukaryotic galactofuranosyltransferases with unprecedented catalytic properties

scientific article published in Scientific Reports

The LPG1x family from Leishmania major is constituted of rare eukaryotic galactofuranosyltransferases with unprecedented catalytic properties is …
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scholarly articleQ13442814

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P356DOI10.1038/S41598-018-35847-W
P932PMC publication ID6279836
P698PubMed publication ID30514885

P50authorPierre LafiteQ58850908
Ryan P SweeneyQ59821462
Cyril ColasQ61163667
Richard DaniellouQ66829672
Todd L. LowaryQ40156801
P2093author name stringRuixiang Blake Zheng
Jihen Ati
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STD-NMR studies suggest that two acceptor substrates for GlfT2, a bifunctional galactofuranosyltransferase required for the biosynthesis of Mycobacterium tuberculosis arabinogalactan, compete for the same binding site.Q45941227
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P275copyright licenseCreative Commons Attribution 4.0 InternationalQ20007257
P6216copyright statuscopyrightedQ50423863
P433issue1
P407language of work or nameEnglishQ1860
P921main subjectLeishmania majorQ1950715
P304page(s)17566
P577publication date2018-12-04
P1433published inScientific ReportsQ2261792
P1476titleThe LPG1x family from Leishmania major is constituted of rare eukaryotic galactofuranosyltransferases with unprecedented catalytic properties
P478volume8