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dc.contributor.authorTerada, T
dc.contributor.authorKitajima, K
dc.contributor.authorInoue, S
dc.contributor.authorWilson, JC
dc.contributor.authorNorton, AK
dc.contributor.authorKong, DCM
dc.contributor.authorThomson, RJ
dc.contributor.authorvonItzstein, M
dc.contributor.authorInoue, Y
dc.date.accessioned2021-04-20T03:39:13Z
dc.date.available2021-04-20T03:39:13Z
dc.date.issued1997
dc.identifier.issn0021-9258
dc.identifier.doi10.1074/jbc.272.9.5452
dc.identifier.urihttp://hdl.handle.net/10072/403856
dc.description.abstractDeaminoneuraminic acid residue-cleaving enzyme (KDNase Sm) is a new sialidase that has been induced and purified from Sphingobacterium multivorum. Catalysis by this new sialidase has been studied by enzyme kinetics and H NMR spectroscopy. V(max)/K(m) values determined for synthetic and natural substrates of KDNase Sm reveal that 4- methylumbelliferyl. KDN (KDNα2MeUmb, V(max)K(m) = 0.033 min ) is the best substrate for this sialidase, presumably because of its good leaving group properties. The transition state analogue, 2,3-didehydro-2,3-dideoxy-D- galacto-D-glycero-nonulosonic acid, is a strong competitive inhibitor of KDNase Sm (K(i) = 7.7 μM versus K(m) = 42 μM for KDNα2MeUmb). 2-Deoxy- 2,3-didehydro-N-acetylneuraminic acid and 2-deoxy-2,3-didehydro-N- glycolylneuraminic acid are known to be strong competitive inhibitors for bacterial sialidases such as Arthrobacter ureafaciens sialidase; however, KDNase Sm activity is not significantly inhibited by these compounds. This observation suggests that the hydroxyl group at C-5 is important for recognition of the inhibitor by the enzyme. Reversible addition of water molecule (or hydroxide ion) to the reactive sialosyl cation, presumably formed at the catalytic site of KDNase Sm, eventually gives rise to two different adducts, the α- and β-anomers of free 3-deoxy-D-glycero-D- galacto-nonulosonic acid. H NMR spectroscopic studies clearly demonstrate that the thermodynamically less stable α-form is preferentially formed as the first product of the cleavage reaction and that isomerization rapidly follows, leading to an equilibrium mixture of the two isomers, the β-isomer being the major species at equilibrium. Therefore, we propose that KDNase Sm catalysis proceeds via a mechanism common to the known exosialidases, but the recognition of the substituent at C-5 by the enzyme differs. 1 -1 1
dc.languageEnglish
dc.publisherElsevier
dc.relation.ispartofpagefrom5452
dc.relation.ispartofpageto5456
dc.relation.ispartofissue9
dc.relation.ispartofjournalJournal of Biological Chemistry
dc.relation.ispartofvolume272
dc.subject.fieldofresearchChemical Sciences
dc.subject.fieldofresearchBiological Sciences
dc.subject.fieldofresearchMedical and Health Sciences
dc.subject.fieldofresearchcode03
dc.subject.fieldofresearchcode06
dc.subject.fieldofresearchcode11
dc.subject.keywordsScience & Technology
dc.subject.keywordsLife Sciences & Biomedicine
dc.subject.keywordsBiochemistry & Molecular Biology
dc.subject.keywordsDEAMINATED NEURAMINIC ACID
dc.subject.keywordsRAINBOW-TROUT EGGS
dc.titleCatalysis by a new sialidase, deaminoneuraminic acid residue-cleaving enzyme (KDNase Sm), initially forms a less stable alpha-anomer of 3-deoxy-D-glycero-D-galacto-nonulosonic acid and is strongly inhibited by the transition state analogue, 2-deoxy-2,3-didehydro-D-glycero-D-galacto-2-nonulopyranosonic acid, but not by 2-deoxy-2,3-didehydro-N-acetylneuraminic acid
dc.typeJournal article
dcterms.bibliographicCitationTerada, T; Kitajima, K; Inoue, S; Wilson, JC; Norton, AK; Kong, DCM; Thomson, RJ; vonItzstein, M; Inoue, Y, Catalysis by a new sialidase, deaminoneuraminic acid residue-cleaving enzyme (KDNase Sm), initially forms a less stable alpha-anomer of 3-deoxy-D-glycero-D-galacto-nonulosonic acid and is strongly inhibited by the transition state analogue, 2-deoxy-2,3-didehydro-D-glycero-D-galacto-2-nonulopyranosonic acid, but not by 2-deoxy-2,3-didehydro-N-acetylneuraminic acid, Journal of Biological Chemistry, 1997, 272 (9), pp. 5452-5456
dcterms.licensehttps://creativecommons.org/licenses/by-nc-nd/4.0/
dc.date.updated2021-04-20T03:36:28Z
dc.description.versionVersion of Record (VoR)
gro.rights.copyright© 1997 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. Licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International Licence (http://creativecommons.org/licenses/by-nc-nd/4.0/) which permits unrestricted, non-commercial use, distribution and reproduction in any medium, providing that the work is properly cited.
gro.hasfulltextFull Text
gro.griffith.authorWilson, Jenny C.
gro.griffith.authorThomson, Robin J.
gro.griffith.authorvon Itzstein, Mark


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