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Pyruvate formate lyase is structurally homologous to type I ribonucleotide reductase

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dc.contributor.authorLappaenen, Veli-Matti
dc.contributor.authorMerckel, Michael
dc.contributor.authorOllis, David
dc.contributor.authorWong, Kenny
dc.contributor.authorKozarich, John
dc.contributor.authorGoldman, Adrian
dc.date.accessioned2015-12-13T23:35:11Z
dc.date.issued1999
dc.date.updated2015-12-12T09:39:00Z
dc.description.abstractBackground: Pyruvate formate lyase (PFL) catalyses a key step in Escherichia coli anaerobic glycolysis by converting pyruvate and CoA to formate and acetylCoA. The PFL mechanism involves an unusual radical cleavage of pyruvate, involving an essential Cα
dc.identifier.issn0969-2126
dc.identifier.urihttp://hdl.handle.net/1885/93797
dc.publisherCell Press
dc.sourceStructure
dc.subjectKeywords: bacterial enzyme; lyase; ribonucleotide reductase; article; binding site; catalysis; enzyme analysis; enzyme binding; enzyme mechanism; enzyme structure; escherichia coli; nonhuman; priority journal; structure analysis; Acetyltransferases; Amino Acid Sequ Enzyme mechanism; Pyruvate formate lyase; Ribonucleotide reductase; Structure; X-ray crystallography
dc.titlePyruvate formate lyase is structurally homologous to type I ribonucleotide reductase
dc.typeJournal article
local.bibliographicCitation.issue7
local.bibliographicCitation.lastpage744
local.bibliographicCitation.startpage733
local.contributor.affiliationLappaenen, Veli-Matti, University of Turku
local.contributor.affiliationMerckel, Michael, University of Turku
local.contributor.affiliationOllis, David, College of Physical and Mathematical Sciences, ANU
local.contributor.affiliationWong, Kenny, Merck Research Laboratories
local.contributor.affiliationKozarich, John, Merck Research Laboratories
local.contributor.affiliationGoldman, Adrian, University of Turku
local.contributor.authoruidOllis, David, u9200080
local.description.embargo2037-12-31
local.description.notesImported from ARIES
local.description.refereedYes
local.identifier.absfor030499 - Medicinal and Biomolecular Chemistry not elsewhere classified
local.identifier.ariespublicationMigratedxPub25211
local.identifier.citationvolume7
local.identifier.doi10.1016/S0969-2126(99)80098-7
local.identifier.scopusID2-s2.0-0000062832
local.type.statusPublished Version

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