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Article: The effect of disulfide bond on the conformational stability and catalytic activity of beta-propeller phytase

TitleThe effect of disulfide bond on the conformational stability and catalytic activity of beta-propeller phytase
Authors
KeywordsBacillus
Beta-propeller phytase
Disulfide bond
Phosphorus
Phytate
Issue Date2007
PublisherBentham Science Publishers Ltd. The Journal's web site is located at http://www.bentham.org/ppl/index.htm
Citation
Protein And Peptide Letters, 2007, v. 14 n. 2, p. 175-183 How to Cite?
AbstractWhile beta-propeller phytases (BPPs) from Gram-positive bacteria do not carry disulfide bonding, their counterparts from Gram-negative bacteria contain cysteine residues that may form disulfide bonds. By molecular modeling, two amino acid residues of B. subtilis 168 phytase (168PhyA), Ser-161 and Leu-212, were mutated to cysteine residues. Although the double cysteine mutant was secreted from B. subtilis at an expression level that was 3.5 times higher than that of the wild type, the biochemical and enzymatic properties were unaltered. In CD spectrometric analysis, both enzymes exhibited similar apparent melting temperatures and mid-points of transition under thermal and guanidine hydrochloride induced denaturation, respectively. In enzyme assays, the mutant phytase exhibited a poor refolding ability after thermal denaturation. We postulate that the disulfide bond in BPP sequences from Gram-negative bacteria is beneficial to their stability in the periplasmic compartment. In contrast, the lack of periplasmic space in Bacillus species and the fact that Bacillus BPPs are released extracellularly may render disulfide bonds unnecessary. This may explain why in evolution, BPPs in Bacillus species do not carry disulfide bonds. © 2007 Bentham Science Publishers Ltd.
Persistent Identifierhttp://hdl.handle.net/10722/84870
ISSN
2015 Impact Factor: 1.069
2015 SCImago Journal Rankings: 0.472
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorCheng, Cen_HK
dc.contributor.authorWong, KBen_HK
dc.contributor.authorLim, BLen_HK
dc.date.accessioned2010-09-06T08:58:05Z-
dc.date.available2010-09-06T08:58:05Z-
dc.date.issued2007en_HK
dc.identifier.citationProtein And Peptide Letters, 2007, v. 14 n. 2, p. 175-183en_HK
dc.identifier.issn0929-8665en_HK
dc.identifier.urihttp://hdl.handle.net/10722/84870-
dc.description.abstractWhile beta-propeller phytases (BPPs) from Gram-positive bacteria do not carry disulfide bonding, their counterparts from Gram-negative bacteria contain cysteine residues that may form disulfide bonds. By molecular modeling, two amino acid residues of B. subtilis 168 phytase (168PhyA), Ser-161 and Leu-212, were mutated to cysteine residues. Although the double cysteine mutant was secreted from B. subtilis at an expression level that was 3.5 times higher than that of the wild type, the biochemical and enzymatic properties were unaltered. In CD spectrometric analysis, both enzymes exhibited similar apparent melting temperatures and mid-points of transition under thermal and guanidine hydrochloride induced denaturation, respectively. In enzyme assays, the mutant phytase exhibited a poor refolding ability after thermal denaturation. We postulate that the disulfide bond in BPP sequences from Gram-negative bacteria is beneficial to their stability in the periplasmic compartment. In contrast, the lack of periplasmic space in Bacillus species and the fact that Bacillus BPPs are released extracellularly may render disulfide bonds unnecessary. This may explain why in evolution, BPPs in Bacillus species do not carry disulfide bonds. © 2007 Bentham Science Publishers Ltd.en_HK
dc.languageengen_HK
dc.publisherBentham Science Publishers Ltd. The Journal's web site is located at http://www.bentham.org/ppl/index.htmen_HK
dc.relation.ispartofProtein and Peptide Lettersen_HK
dc.subjectBacillusen_HK
dc.subjectBeta-propeller phytaseen_HK
dc.subjectDisulfide bonden_HK
dc.subjectPhosphorusen_HK
dc.subjectPhytateen_HK
dc.titleThe effect of disulfide bond on the conformational stability and catalytic activity of beta-propeller phytaseen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0929-8665&volume=14&spage=175&epage=183&date=2007&atitle=The+Effect+of+Disulfide+Bond+on+the+Conformational+Stability+and+Catalytic+Activity+of+Beta-Propeller+Phytaseen_HK
dc.identifier.emailLim, BL: bllim@hkucc.hku.hken_HK
dc.identifier.authorityLim, BL=rp00744en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.2174/092986607779816069en_HK
dc.identifier.pmid17305605-
dc.identifier.scopuseid_2-s2.0-33846953250en_HK
dc.identifier.hkuros126282en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-33846953250&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume14en_HK
dc.identifier.issue2en_HK
dc.identifier.spage175en_HK
dc.identifier.epage183en_HK
dc.identifier.isiWOS:000245114800011-
dc.publisher.placeNetherlandsen_HK
dc.identifier.scopusauthoridCheng, C=7404797223en_HK
dc.identifier.scopusauthoridWong, KB=7404759301en_HK
dc.identifier.scopusauthoridLim, BL=7201983917en_HK
dc.identifier.citeulike1086767-

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