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2016-03-10Zeitschriftenartikel DOI: 10.1159/000440882
Structure and Function of 4-Hydroxyphenylacetate Decarboxylase and Its Cognate Activating Enzyme
dc.contributor.authorSelvaraj, Brinda
dc.contributor.authorBuckel, Wolfgang
dc.contributor.authorGolding, Bernard T.
dc.contributor.authorUllmann, Matthias
dc.contributor.authorMartins, Berta
dc.date.accessioned2019-11-20T10:31:22Z
dc.date.available2019-11-20T10:31:22Z
dc.date.issued2016-03-10none
dc.date.updated2019-09-23T13:50:14Z
dc.identifier26959876
dc.identifier.issn1464-1801
dc.identifier.urihttp://edoc.hu-berlin.de/18452/21521
dc.description.abstract4-Hydroxyphenylacetate decarboxylase (4Hpad) is the prototype of a new class of Fe-S cluster-dependent glycyl radical enzymes (Fe-S GREs) acting on aromatic compounds. The two-enzyme component system comprises a decarboxylase responsible for substrate conversion and a dedicated activating enzyme (4Hpad-AE). The decarboxylase uses a glycyl/thiyl radical dyad to convert 4-hydroxyphenylacetate into p-cresol (4-methylphenol) by a biologically unprecedented Kolbe-type decarboxylation. In addition to the radical dyad prosthetic group, the decarboxylase unit contains two [4Fe-4S] clusters coordinated by an extra small subunit of unknown function. 4Hpad-AE reductively cleaves S-adenosylmethionine (SAM or AdoMet) at a site-differentiated [4Fe-4S]<sup>2+/+</sup> cluster (RS cluster) generating a transient 5′-deoxyadenosyl radical that produces a stable glycyl radical in the decarboxylase by the abstraction of a hydrogen atom. 4Hpad-AE binds up to two auxiliary [4Fe-4S] clusters coordinated by a ferredoxin-like insert that is C-terminal to the RS cluster-binding motif. The ferredoxin-like domain with its two auxiliary clusters is not vital for SAM-dependent glycyl radical formation in the decarboxylase, but facilitates a longer lifetime for the radical. This review describes the 4Hpad and cognate AE families and focuses on the recent advances and open questions concerning the structure, function and mechanism of this novel Fe-S-dependent class of GREs.eng
dc.language.isoengnone
dc.publisherHumboldt-Universität zu Berlin
dc.rights.urihttp://rightsstatements.org/vocab/InC/1.0/
dc.subjectAromatic degradationeng
dc.subject4-Methylphenoleng
dc.subjectCresoleng
dc.subjectS-adenosylmethionineeng
dc.subjectGlycyl radical enzymeseng
dc.subjectRadical catalysiseng
dc.subjectFe-S clustereng
dc.subjectC-C bond cleavageeng
dc.subject.ddc570 Biologienone
dc.titleStructure and Function of 4-Hydroxyphenylacetate Decarboxylase and Its Cognate Activating Enzymenone
dc.typearticle
dc.identifier.urnurn:nbn:de:kobv:11-110-18452/21521-1
dc.identifier.doi10.1159/000440882none
dc.identifier.doihttp://dx.doi.org/10.18452/20783
dc.type.versionpublishedVersionnone
local.edoc.container-titleJournal of Molecular Microbiology and Biotechnologynone
local.edoc.pages16none
local.edoc.anmerkungThis publication is with permission of the rights owner freely accessible due to an alliance licence and a national licence (funded by the DFG, German Research Foundation) respectively.none
local.edoc.type-nameZeitschriftenartikel
local.edoc.institutionLebenswissenschaftliche Fakultätnone
local.edoc.container-typeperiodical
local.edoc.container-type-nameZeitschrift
local.edoc.container-publisher-nameS. Karger AGnone
local.edoc.container-publisher-placeBasel, Switzerlandnone
local.edoc.container-volume26none
local.edoc.container-issue1-3none
local.edoc.container-firstpage76none
local.edoc.container-lastpage91none
dc.description.versionPeer Reviewednone
dc.identifier.eissn1660-2412

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