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Article: Crystal structures of Fms1 and its complex with spermine reveal substrate specificity

TitleCrystal structures of Fms1 and its complex with spermine reveal substrate specificity
Authors
KeywordsCrystal structure
Fms1
Polyamine oxidase
SAD
Spermine
Issue Date2005
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/jmb
Citation
Journal Of Molecular Biology, 2005, v. 348 n. 4, p. 951-959 How to Cite?
AbstractFms1 is a rate-limiting enzyme for the biosynthesis of pantothenic acid in yeast. Fms1 has polyamine oxidase (PAO) activity, which converts spermine into spermidine and 3-aminopropanal. The 3-aminopropanal is further oxidized to produce β-alanine, which is necessary for the biosynthesis of pantothenic acid. The crystal structures of Fms1 and its complex with the substrate spermine have been determined using the single-wavelength anomalous diffraction (SAD) phasing method. Fms1 consists of an FAD-binding domain, with Rossmann fold topology, and a substrate-binding domain. The active site is a tunnel located at the interface of the two domains. The substrate spermine binds to the active site mainly via hydrogen bonds and hydrophobic interactions. In the complex, C11 but not C9 of spermine is close enough to the catalytic site (N5 of FAD) to be oxidized. Therefore, the products are spermidine and 3-aminopropanal, rather than 3-(aminopropyl) 4-aminobutyraldehyde and 1,3-diaminoprone. © 2005 Elsevier Ltd. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/91934
ISSN
2015 Impact Factor: 4.517
2015 SCImago Journal Rankings: 3.002
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorHuang, Qen_HK
dc.contributor.authorLiu, Qen_HK
dc.contributor.authorHao, Qen_HK
dc.date.accessioned2010-09-17T10:30:58Z-
dc.date.available2010-09-17T10:30:58Z-
dc.date.issued2005en_HK
dc.identifier.citationJournal Of Molecular Biology, 2005, v. 348 n. 4, p. 951-959en_HK
dc.identifier.issn0022-2836en_HK
dc.identifier.urihttp://hdl.handle.net/10722/91934-
dc.description.abstractFms1 is a rate-limiting enzyme for the biosynthesis of pantothenic acid in yeast. Fms1 has polyamine oxidase (PAO) activity, which converts spermine into spermidine and 3-aminopropanal. The 3-aminopropanal is further oxidized to produce β-alanine, which is necessary for the biosynthesis of pantothenic acid. The crystal structures of Fms1 and its complex with the substrate spermine have been determined using the single-wavelength anomalous diffraction (SAD) phasing method. Fms1 consists of an FAD-binding domain, with Rossmann fold topology, and a substrate-binding domain. The active site is a tunnel located at the interface of the two domains. The substrate spermine binds to the active site mainly via hydrogen bonds and hydrophobic interactions. In the complex, C11 but not C9 of spermine is close enough to the catalytic site (N5 of FAD) to be oxidized. Therefore, the products are spermidine and 3-aminopropanal, rather than 3-(aminopropyl) 4-aminobutyraldehyde and 1,3-diaminoprone. © 2005 Elsevier Ltd. All rights reserved.en_HK
dc.languageengen_HK
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/jmben_HK
dc.relation.ispartofJournal of Molecular Biologyen_HK
dc.subjectCrystal structureen_HK
dc.subjectFms1en_HK
dc.subjectPolyamine oxidaseen_HK
dc.subjectSADen_HK
dc.subjectSpermineen_HK
dc.titleCrystal structures of Fms1 and its complex with spermine reveal substrate specificityen_HK
dc.typeArticleen_HK
dc.identifier.emailHao, Q: qhao@hku.hken_HK
dc.identifier.authorityHao, Q=rp01332en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.jmb.2005.03.008en_HK
dc.identifier.pmid15843025-
dc.identifier.scopuseid_2-s2.0-17444422874en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-17444422874&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume348en_HK
dc.identifier.issue4en_HK
dc.identifier.spage951en_HK
dc.identifier.epage959en_HK
dc.identifier.isiWOS:000228876400013-
dc.publisher.placeUnited Kingdomen_HK
dc.deduplication.noteHao, Qen_US
dc.identifier.scopusauthoridHuang, Q=7403634448en_HK
dc.identifier.scopusauthoridLiu, Q=35215401600en_HK
dc.identifier.scopusauthoridHao, Q=7102508868en_HK

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