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Substrate interaction with recombinant amidase from Pseudomonas aeruginosa during biocatalysis

2009Journal article Open access
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dc.contributor.authorPacheco, Rita
dc.contributor.authorKarmali, Amin
dc.contributor.authorSerralheiro, Maria Luísa M.
dc.contributor.authorHaris, Parvez I.
dc.date.accessioned2012-03-23T16:29:35Z
dc.date.available2012-03-23T16:29:35Z
dc.date.issued2009
dc.description.abstractThe interaction of a variety of substrates with Pseudomonas aeruginosa native amidase (E.C. 3.5.1.4), overproduced in an Escherichia coli strain, was investigated using difference FTIR spectroscopy. The amides used as substrates showed an increase in hydrogen bonding upon association in multimers, which was not seen with esters. Evidence for an overall reduction or weakening of hydrogen bonding while amide and ester substrates are interacting with the enzyme is presented. The results describe a spectroscopic approach for analysis of substrate-amidase interaction and in situ monitoring of the hydrolysis and transferase reaction when amides or esters are used as substrates.por
dc.identifier.citationPacheco R, Karmali A, Serralheiro M L M, Haris P I. Substrate interaction with recombinant amidase from Pseudomonas aeruginosa during biocatalysis. Biocatalys and Biotransformation. 2009; 27 (5-6): 367-376.por
dc.identifier.issn1024-2422
dc.identifier.urihttp://hdl.handle.net/10400.21/1362
dc.language.isoengpor
dc.peerreviewedyespor
dc.publisherTaylor & Francis LTDpor
dc.relation.ispartofseries5-6
dc.subjectRecombinant Amidasepor
dc.subjectDifference FTIR spectroscopypor
dc.subjectSubstrates interactionpor
dc.subjectCatalytic mechanismpor
dc.subjectTransform infrared-spectroscopypor
dc.subjectHuman serum-albuminpor
dc.subjectMolecular interpretationpor
dc.subjectDifference spectrapor
dc.subjectEnzymatic-activitypor
dc.subjectActive-sitepor
dc.subjectBindingpor
dc.subjectFTIRpor
dc.subjectATPpor
dc.subjectHydrolysispor
dc.titleSubstrate interaction with recombinant amidase from Pseudomonas aeruginosa during biocatalysispor
dc.typejournal article
dspace.entity.typePublication
oaire.citation.conferencePlaceOxonpor
oaire.citation.endPage376por
oaire.citation.issue27por
oaire.citation.startPage367por
oaire.citation.titleBiocatalys and Biotransformationpor
person.familyNamePacheco
person.familyNameKarmali
person.givenNameRita
person.givenNameAmin
person.identifier1022927
person.identifier.ciencia-id9F13-D310-B5A3
person.identifier.orcid0000-0001-5192-3006
person.identifier.orcid0000-0003-0419-401X
person.identifier.ridC-3062-2012
person.identifier.ridE-4787-2011
person.identifier.scopus-author-id8853708300
person.identifier.scopus-author-id6603778216
rcaap.rightsrestrictedAccesspor
rcaap.typearticlepor
relation.isAuthorOfPublicationd6907c0a-3f8f-431c-acf2-0b257692f0d4
relation.isAuthorOfPublication23975b4b-3234-4139-9675-89ea6f9a2332
relation.isAuthorOfPublication.latestForDiscoveryd6907c0a-3f8f-431c-acf2-0b257692f0d4

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