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Article: Characterization of His-tagged rat uroporphyrinogen III synthase wild-type and variant enzymes
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TitleCharacterization of His-tagged rat uroporphyrinogen III synthase wild-type and variant enzymes
 
AuthorsLi, N1
Ma, DL2
Liu, X1
Wu, L1
Chu, X1
Wong, KY2
Li, D1
 
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
 
CitationProtein Journal, 2007, v. 26 n. 8, p. 569-576 [How to Cite?]
DOI: http://dx.doi.org/10.1007/s10930-007-9099-7
 
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.
 
ISSN1572-3887
2013 Impact Factor: 1.039
2013 SCImago Journal Rankings: 0.466
 
DOIhttp://dx.doi.org/10.1007/s10930-007-9099-7
 
ReferencesReferences in Scopus
 
DC FieldValue
dc.contributor.authorLi, N
 
dc.contributor.authorMa, DL
 
dc.contributor.authorLiu, X
 
dc.contributor.authorWu, L
 
dc.contributor.authorChu, X
 
dc.contributor.authorWong, KY
 
dc.contributor.authorLi, D
 
dc.date.accessioned2012-10-08T03:15:43Z
 
dc.date.available2012-10-08T03:15:43Z
 
dc.date.issued2007
 
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.
 
dc.description.naturelink_to_subscribed_fulltext
 
dc.identifier.citationProtein Journal, 2007, v. 26 n. 8, p. 569-576 [How to Cite?]
DOI: http://dx.doi.org/10.1007/s10930-007-9099-7
 
dc.identifier.doihttp://dx.doi.org/10.1007/s10930-007-9099-7
 
dc.identifier.epage576
 
dc.identifier.issn1572-3887
2013 Impact Factor: 1.039
2013 SCImago Journal Rankings: 0.466
 
dc.identifier.issue8
 
dc.identifier.pmid17763925
 
dc.identifier.scopuseid_2-s2.0-35848970354
 
dc.identifier.spage569
 
dc.identifier.urihttp://hdl.handle.net/10722/168151
 
dc.identifier.volume26
 
dc.languageeng
 
dc.publisherSpringer New York LLC. The Journal's web site is located at http://springerlink.metapress.com/openurl.asp?genre=journal&issn=1572-3887
 
dc.publisher.placeUnited States
 
dc.relation.ispartofProtein Journal
 
dc.relation.referencesReferences in Scopus
 
dc.subject.meshAmino Acid Sequence
 
dc.subject.meshAnimals
 
dc.subject.meshBinding Sites
 
dc.subject.meshCatalysis
 
dc.subject.meshCloning, Molecular
 
dc.subject.meshCrystallography, X-Ray
 
dc.subject.meshGene Library
 
dc.subject.meshHistidine - Chemistry
 
dc.subject.meshLiver - Enzymology
 
dc.subject.meshModels, Molecular
 
dc.subject.meshMolecular Sequence Data
 
dc.subject.meshMutagenesis, Site-Directed
 
dc.subject.meshProtein Conformation
 
dc.subject.meshRats
 
dc.subject.meshSequence Homology, Amino Acid
 
dc.subject.meshSubstrate Specificity
 
dc.subject.meshUroporphyrinogen Iii Synthetase - Chemistry - Genetics - Metabolism
 
dc.titleCharacterization of His-tagged rat uroporphyrinogen III synthase wild-type and variant enzymes
 
dc.typeArticle
 
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<contributor.author>Chu, X</contributor.author>
<contributor.author>Wong, KY</contributor.author>
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<description.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 &#197; away from the D ring, and is within hydrogen bond distance (1.9 &#197;) with acetate side chain of the D ring. &#169; 2007 Springer Science+Business Media, LLC.</description.abstract>
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Author Affiliations
  1. City University of Hong Kong
  2. Hong Kong Polytechnic University