Please use this identifier to cite or link to this item: https://doi.org/10.1021/bi801876q
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dc.titleThe missing link in petrobactin biosynthesis: asbF encodes a (-)-3-dehydroshikimate dehydratase
dc.contributor.authorFox, D.T.
dc.contributor.authorHotta, K.
dc.contributor.authorKim, C.-Y.
dc.contributor.authorKoppisch, A.T.
dc.date.accessioned2014-10-27T08:43:03Z
dc.date.available2014-10-27T08:43:03Z
dc.date.issued2008-11-25
dc.identifier.citationFox, D.T., Hotta, K., Kim, C.-Y., Koppisch, A.T. (2008-11-25). The missing link in petrobactin biosynthesis: asbF encodes a (-)-3-dehydroshikimate dehydratase. Biochemistry 47 (47) : 12251-12253. ScholarBank@NUS Repository. https://doi.org/10.1021/bi801876q
dc.identifier.issn00062960
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/101966
dc.description.abstractThe siderophore petrobactin harbors unique 3,4-dihydroxybenzoyl iron-liganding groups. These moieties are known to be synthesized from shikimate pathway precursors, but no reports of the biosynthetic enzymes responsible for this conversion have been published. The gene encoding AsbF from Bacillus thuringiensis 97-27 was overexpressed in an Escherichia coli host. AsbF rapidly and efficiently transforms (-)-3-dehydroshikimate (DHS) into 3,4-dihydroxybenzoate (kcat DHS = 217 ± 10 min -1; Km DHS = 125 ± 14 μM) at 37°C and has an absolute requirement for divalent metal. Finally, the pH versus kcat DHS profile revealed two ionizable groups (pK a1 = 7.9 ± 0.1, and pKa2 = 9.3 ± 0.1). © 2008 American Chemical Society.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1021/bi801876q
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1021/bi801876q
dc.description.sourcetitleBiochemistry
dc.description.volume47
dc.description.issue47
dc.description.page12251-12253
dc.description.codenBICHA
dc.identifier.isiut000261000100001
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