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Article: Crystallographic snapshots of Aspergillus fumigatus phytase, revealing its enzymatic dynamics

TitleCrystallographic snapshots of Aspergillus fumigatus phytase, revealing its enzymatic dynamics
Authors
KeywordsSpecies Index: Aspergillus
Aspergillus Fumigatus
Issue Date2004
PublisherCell Press. The Journal's web site is located at http://www.elsevier.com/locate/str
Citation
Structure, 2004, v. 12 n. 9, p. 1575-1583 How to Cite?
AbstractUnderstanding of the atomic movements involved in an enzymatic reaction needs structural information on the active and inactive native enzyme molecules and on the enzyme-substrate, enzyme-intermediate, and enzyme-product(s) complexes. By using the X-ray crystallographic method, four crystal structures of Aspergillus fumigatus phytase were obtained at resolution higher than 1.7 Å. The pH-dependent catalytic activity of A. fumigatus phytase was linked to three water molecules that may prevent the substrate from binding and thus block nucleophilic attack of the catalytic imidazole nitrogen. Comparison of various structures also identified the water molecule that attacks the phosphamide bond during the hydrolysis process, and established the hydrolysis pathway of the intermediate. Additionally, two reaction product phosphates were observed at the active site, suggesting a possible product release pathway after hydrolysis of the intermediate. These results can help explain the catalytic mechanism throughout the whole acid phosphatase family, as all key residues are conserved.
Persistent Identifierhttp://hdl.handle.net/10722/91947
ISSN
2015 Impact Factor: 5.237
2015 SCImago Journal Rankings: 4.770
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLiu, Qen_HK
dc.contributor.authorHuang, Qen_HK
dc.contributor.authorLei, XGen_HK
dc.contributor.authorHao, Qen_HK
dc.date.accessioned2010-09-17T10:31:22Z-
dc.date.available2010-09-17T10:31:22Z-
dc.date.issued2004en_HK
dc.identifier.citationStructure, 2004, v. 12 n. 9, p. 1575-1583en_HK
dc.identifier.issn0969-2126en_HK
dc.identifier.urihttp://hdl.handle.net/10722/91947-
dc.description.abstractUnderstanding of the atomic movements involved in an enzymatic reaction needs structural information on the active and inactive native enzyme molecules and on the enzyme-substrate, enzyme-intermediate, and enzyme-product(s) complexes. By using the X-ray crystallographic method, four crystal structures of Aspergillus fumigatus phytase were obtained at resolution higher than 1.7 Å. The pH-dependent catalytic activity of A. fumigatus phytase was linked to three water molecules that may prevent the substrate from binding and thus block nucleophilic attack of the catalytic imidazole nitrogen. Comparison of various structures also identified the water molecule that attacks the phosphamide bond during the hydrolysis process, and established the hydrolysis pathway of the intermediate. Additionally, two reaction product phosphates were observed at the active site, suggesting a possible product release pathway after hydrolysis of the intermediate. These results can help explain the catalytic mechanism throughout the whole acid phosphatase family, as all key residues are conserved.en_HK
dc.languageengen_HK
dc.publisherCell Press. The Journal's web site is located at http://www.elsevier.com/locate/stren_HK
dc.relation.ispartofStructureen_HK
dc.subjectSpecies Index: Aspergillusen_HK
dc.subjectAspergillus Fumigatusen_HK
dc.titleCrystallographic snapshots of Aspergillus fumigatus phytase, revealing its enzymatic dynamicsen_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.str.2004.06.015en_HK
dc.identifier.pmid15341723-
dc.identifier.scopuseid_2-s2.0-4444336413en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-4444336413&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume12en_HK
dc.identifier.issue9en_HK
dc.identifier.spage1575en_HK
dc.identifier.epage1583en_HK
dc.identifier.isiWOS:000223969500003-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridLiu, Q=35215401600en_HK
dc.identifier.scopusauthoridHuang, Q=7403634448en_HK
dc.identifier.scopusauthoridLei, XG=7202627277en_HK
dc.identifier.scopusauthoridHao, Q=7102508868en_HK

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