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Article: Characterization of His-tagged rat uroporphyrinogen III synthase wild-type and variant enzymes

TitleCharacterization of His-tagged rat uroporphyrinogen III synthase wild-type and variant enzymes
Authors
Issue Date2007
PublisherSpringer New York LLC. The Journal's web site is located at http://springerlink.metapress.com/openurl.asp?genre=journal&issn=1572-3887
Citation
Protein Journal, 2007, v. 26 n. 8, p. 569-576 How to Cite?
Abstract
The structurally related tetrapyrrolic pigments are a group of natural products that participate in many of the fundamental biosynthetic and catabolic processes of living organisms. Urogen III synthase catalyzes a key step in the formation of urogen III, a common intermediate for tetrapyrrolic natural products. In the present study, we cloned, purified, and characterized His-tagged rat urogen III synthase. The mechanism of enzymatic reaction was studied through site-directed mutagenesis of eight highly conserved residues with functional side chains around the active site followed with activity tests. Lys10, Asp17, Glu68, Tyr97, Asn121, Lys147, and His173 have not been studied previously, which were found to be unessential for enzymatic reaction. Tyr168 was identified as an important residue for enzymatic reaction catalyzed by rat urogen III synthase. Molecular modeling suggests the hydroxyl group of Tyr168 side chain is 3.5 Å away from the D ring, and is within hydrogen bond distance (1.9 Å) with acetate side chain of the D ring. © 2007 Springer Science+Business Media, LLC.
Persistent Identifierhttp://hdl.handle.net/10722/168151
ISSN
2013 Impact Factor: 1.039
2013 SCImago Journal Rankings: 0.466
ISI Accession Number ID
References

 

Author Affiliations
  1. City University of Hong Kong
  2. Hong Kong Polytechnic University
DC FieldValueLanguage
dc.contributor.authorLi, Nen_US
dc.contributor.authorMa, DLen_US
dc.contributor.authorLiu, Xen_US
dc.contributor.authorWu, Len_US
dc.contributor.authorChu, Xen_US
dc.contributor.authorWong, KYen_US
dc.contributor.authorLi, Den_US
dc.date.accessioned2012-10-08T03:15:43Z-
dc.date.available2012-10-08T03:15:43Z-
dc.date.issued2007en_US
dc.identifier.citationProtein Journal, 2007, v. 26 n. 8, p. 569-576en_US
dc.identifier.issn1572-3887en_US
dc.identifier.urihttp://hdl.handle.net/10722/168151-
dc.description.abstractThe structurally related tetrapyrrolic pigments are a group of natural products that participate in many of the fundamental biosynthetic and catabolic processes of living organisms. Urogen III synthase catalyzes a key step in the formation of urogen III, a common intermediate for tetrapyrrolic natural products. In the present study, we cloned, purified, and characterized His-tagged rat urogen III synthase. The mechanism of enzymatic reaction was studied through site-directed mutagenesis of eight highly conserved residues with functional side chains around the active site followed with activity tests. Lys10, Asp17, Glu68, Tyr97, Asn121, Lys147, and His173 have not been studied previously, which were found to be unessential for enzymatic reaction. Tyr168 was identified as an important residue for enzymatic reaction catalyzed by rat urogen III synthase. Molecular modeling suggests the hydroxyl group of Tyr168 side chain is 3.5 Å away from the D ring, and is within hydrogen bond distance (1.9 Å) with acetate side chain of the D ring. © 2007 Springer Science+Business Media, LLC.en_US
dc.languageengen_US
dc.publisherSpringer New York LLC. The Journal's web site is located at http://springerlink.metapress.com/openurl.asp?genre=journal&issn=1572-3887en_US
dc.relation.ispartofProtein Journalen_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshAnimalsen_US
dc.subject.meshBinding Sitesen_US
dc.subject.meshCatalysisen_US
dc.subject.meshCloning, Molecularen_US
dc.subject.meshCrystallography, X-Rayen_US
dc.subject.meshGene Libraryen_US
dc.subject.meshHistidine - Chemistryen_US
dc.subject.meshLiver - Enzymologyen_US
dc.subject.meshModels, Molecularen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshMutagenesis, Site-Directeden_US
dc.subject.meshProtein Conformationen_US
dc.subject.meshRatsen_US
dc.subject.meshSequence Homology, Amino Aciden_US
dc.subject.meshSubstrate Specificityen_US
dc.subject.meshUroporphyrinogen Iii Synthetase - Chemistry - Genetics - Metabolismen_US
dc.titleCharacterization of His-tagged rat uroporphyrinogen III synthase wild-type and variant enzymesen_US
dc.typeArticleen_US
dc.identifier.emailMa, DL:edmondma@hku.hken_US
dc.identifier.authorityMa, DL=rp00760en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1007/s10930-007-9099-7en_US
dc.identifier.pmid17763925en_US
dc.identifier.scopuseid_2-s2.0-35848970354en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-35848970354&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume26en_US
dc.identifier.issue8en_US
dc.identifier.spage569en_US
dc.identifier.epage576en_US
dc.identifier.isiWOS:000250722600007-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridLi, N=36064475400en_US
dc.identifier.scopusauthoridMa, DL=7402075538en_US
dc.identifier.scopusauthoridLiu, X=26428187400en_US
dc.identifier.scopusauthoridWu, L=11640415600en_US
dc.identifier.scopusauthoridChu, X=7102057236en_US
dc.identifier.scopusauthoridWong, KY=7404760030en_US
dc.identifier.scopusauthoridLi, D=26643209100en_US

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