Sökning: id:"swepub:oai:DiVA.org:kth-16010" >
Transferase and hyd...
Transferase and hydrolytic activities of the laminarinase from rhodothermus marinus and its M133A, M133C, and M133W mutants
-
Neustroev, Kirill N. (författare)
-
Golubev, Alexander M. (författare)
-
Sinnott, Michael L. (författare)
-
visa fler...
-
Borriss, Rainer (författare)
-
Krah, Martin (författare)
-
Brumer, Harry, III (författare)
-
Eneyskaya, Elena V. (författare)
-
Shishlyannikov, Sergey (författare)
-
Shabalin, Konstantin A. (författare)
-
Peshechonov, Viacheslav T. (författare)
-
Korolev, Vladimir G. (författare)
-
Kulminskaya, Anna A. (författare)
-
visa färre...
- Springer Science and Business Media LLC, 2006
- 2006
- Engelska.
-
Ingår i: Glycoconjugate Journal. - : Springer Science and Business Media LLC. - 0282-0080 .- 1573-4986. ; 23:08-jul, s. 501-511
- Relaterad länk:
-
https://urn.kb.se/re...
-
visa fler...
-
https://doi.org/10.1...
-
visa färre...
Abstract
Ämnesord
Stäng
- Comparative studies of the transglycosylation and hydrolytic activities have been performed on the Rhodothermus marinus beta-1,3-glucanase (laminarinase) and its M133A, M133C, and M133W mutants. The M133C mutant demonstrated near 20% greater rate of transglycosylation activity in comparison with the M133A and M133W mutants that was measured by NMR quantitation of nascent beta(1-4) and beta(1-6) linkages. To obtain kinetic probes for the wild-type enzyme and Met-133 mutants, p-nitrophenyl beta-laminarin oligosaccharides of degree of polymerisation 2-8 were synthesized enzymatically. Catalytic efficiency values, k (cat)/K (m), of the laminarinase catalysed hydrolysis of these oligosaccharides suggested possibility of four negative and at least three positive binding subsites in the active site. Comparison of action patterns of the wild-type and M133C mutant in the hydrolysis of the p-nitrophenyl-beta-D-oligosac- charides indicated that the increased transglycosylation activity of the M133C mutant did not result from altered subsite affinities. The stereospecificity of the transglycosylation reaction also was unchanged in all mutants; the major transglycosylation products in hydrolysis of p-nitrophenyl laminaribioside were beta-glucopyranosyl-beta-1,3-D-glucopy- ranosyl-beta-1,3-D-glucopyranose and beta-glucopyranosyl-beta-1, 3-D-glucopyranosyl-beta-1,3-D-glucpyranosyl-beta-1,3-D- glucopyranoxside.
Nyckelord
- laminarinase
- Rhodothermus marinus
- p-nitrophenyl beta-laminarin oligosaccharides
- transglycosylation
- bacillus 1,3-1,4-beta-d-glucan 4-glucanohydrolases
- oligosaccharide synthesis
- enzymatic-synthesis
- transglycosylation activity
- aspergillus-niger
- beta-glucosidase
- alpha-amylase
- active-site
- mechanism
- (1->3)-beta-d-glucan
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
Hitta via bibliotek
Till lärosätets databas
- Av författaren/redakt...
-
Neustroev, Kiril ...
-
Golubev, Alexand ...
-
Sinnott, Michael ...
-
Borriss, Rainer
-
Krah, Martin
-
Brumer, Harry, I ...
-
visa fler...
-
Eneyskaya, Elena ...
-
Shishlyannikov, ...
-
Shabalin, Konsta ...
-
Peshechonov, Via ...
-
Korolev, Vladimi ...
-
Kulminskaya, Ann ...
-
visa färre...
- Artiklar i publikationen
-
Glycoconjugate J ...
- Av lärosätet
-
Kungliga Tekniska Högskolan