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dc.contributor.authorPoppe, Juliane
dc.contributor.authorReichelt, Joachim
dc.contributor.authorBlankenfeldt, Wulf
dc.date.accessioned2018-11-06T09:49:44Z
dc.date.available2018-11-06T09:49:44Z
dc.date.issued2018-09-21
dc.identifier.issn1083-351X
dc.identifier.pmid30030378
dc.identifier.doi10.1074/jbc.RA118.002560
dc.identifier.urihttp://hdl.handle.net/10033/621538
dc.description.abstractPyoverdines (PVDs) are important chromophore-containing siderophores of fluorescent pseudomonad bacteria such as the opportunistic human pathogenen_US
dc.rightsAttribution-NonCommercial-ShareAlike 3.0 United States*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/3.0/us/*
dc.subjectPseudomonas aeruginosa (P. aeruginosa)en_US
dc.subjectbiosynthesisen_US
dc.subjectcopperen_US
dc.subjectenzymeen_US
dc.subjectinfectious diseaseen_US
dc.subjectprotein structureen_US
dc.subjectsiderophoreen_US
dc.subjectstreptavidinen_US
dc.subjecttyrosinaseen_US
dc.titlePseudomonas aeruginosa pyoverdine maturation enzyme PvdP has a noncanonical domain architecture and affords insight into a new subclass of tyrosinasesen_US
dc.typeArticleen_US
dc.contributor.departmentHZI,Helmholtz-Zentrum für Infektionsforschung GmbH, Inhoffenstr. 7,38124 Braunschweig, Germany.en_US
dc.source.journaltitleThe Journal of biological chemistry


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