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O-Methyltransferase Is Shared between the Pentose Phosphate and Shikimate Pathways and Is Essential for Mycosporine-Like Amino Acid Biosynthesis in Anabaena variabilis ATCC 29413

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dc.contributor Prote Facil
dc.contributor University Of Maine Orono
dc.contributor Australian Inst Marine Sci
dc.contributor Ucl Sch Pharm
dc.contributor Sch Marine Sci
dc.contributor Univ Maine
dc.contributor Ctr Marine Microbiol & Genet
dc.contributor University Of Maine System
dc.contributor Inst Psychiat Psychol & Neurosci
dc.contributor Dept Chem
dc.contributor Kings College London
dc.contributor Australian Institute Of Marine Science
dc.contributor Dept Biol Chem
dc.contributor University Of London
dc.contributor University Of Maine
dc.contributor University College London
dc.contributor Inst Pharmaceut Sci
dc.contributor Kings Coll London LONG, PAUL F. POPE, MATTHEW A. SPENCE, EDWARD SERALVO, VALENTINA GACESA, RANKO HEIDELBERGER, SIBYLLE WESTON, ANDREW J. DUNLAP, WALTER C. SHICK, J. MALCOLM 2017-03-21T01:01:09Z 2017-03-21T01:01:09Z 2015-02-12T05:36:46Z 2019-10-21T21:42:41Z 2015-02-12T05:36:46Z 2017-03-21T01:01:09Z 2015-02-12T05:36:46Z 2019-10-21T21:42:41Z 2015-01-19
dc.identifier.citation Pope MA, Spence E, Seralvo V, Gacesa R, Heidelberger S, Weston AJ, Dunlap WC, Shick JM, Long PF (2015) O-Methyltransferase is shared between the pentose phosphate and shikimate pathways and is essential for mycosporine-like amino acid biosynthesis in Anabaena variabilis ATCC 29413. ChemBioChem 16(2): 320-327 en_US
dc.identifier.issn 1439-4227
dc.description.abstract The parent core structure of mycosporine-like amino acids (MAAs) is 4-deoxygadusol, which, in cyanobacteria, is derived from conversion of the pentose phosphate pathway intermediate sedoheptulose 7-phosphate by the enzymes 2-epi-5-epivaliolone synthase (EVS) and O-methyltransferase (OMT). Yet, deletion of the EVS gene from Anabaena variabilis ATCC 29413 was shown to have little effect on MAA production, thus suggesting that its biosynthesis is not exclusive to the pentose phosphate pathway. Herein, we report how, using pathway-specific inhibitors, we demonstrated unequivocally that MAA biosynthesis occurs also via the shikimate pathway. In addition, complete in-frame gene deletion of the OMT gene from A. variabilis ATCC 29413 reveals that, although biochemically distinct, the pentose phosphate and shikimate pathways are inextricably linked to MAA biosynthesis in this cyanobacterium. Furthermore, proteomic data reveal that the shikimate pathway is the predominate route for UV-induced MAA biosynthesis.
dc.description.sponsorship Financial support for this work came from the Biotechnology and Biological Sciences Research Council of the United Kingdom (BBSRC grant BB/H010009/2 to W.C.D., J.M.S. and P.F.L.).
dc.description.uri en_US
dc.language English
dc.language.iso en en_US
dc.publisher Wiley en_US
dc.relation.ispartof Null
dc.subject Cyanobacterium
dc.subject Biochemistry & Molecular Biology
dc.subject Oxidative Stress
dc.subject Pharmacology & Pharmacy
dc.subject Glutaminol
dc.subject Chemistry, Medicinal
dc.subject Mycosporine-like Amino Acids
dc.subject Pentose Phosphate Pathway
dc.subject Ultraviolet-b Radiation
dc.subject Sunscreen Biosynthesis
dc.subject Nostoc-commune
dc.subject Transaldolase
dc.subject Salt Stress
dc.subject Accumulation
dc.subject Natural Products
dc.subject Statistical-model
dc.subject Microbiology
dc.subject Shikimate Pathway
dc.title O-Methyltransferase Is Shared between the Pentose Phosphate and Shikimate Pathways and Is Essential for Mycosporine-Like Amino Acid Biosynthesis in Anabaena variabilis ATCC 29413
dc.type journal article en_US
dc.identifier.doi 10.1002/cbic.201402516
dc.identifier.wos WOS:000347780800018

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