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Description
  • Fungal b-N-acetylhexosaminidases are inducible extracellular enzymes with many biotechnological applications. The enzyme from Penicillium oxalicum has unique enzymatic properties despite its close evolutionary relationship with other fungal hexosaminidases. It has high GalNAcase activity, tolerates substrates with the modified N-acyl group better and has some other unusual catalytic properties. In order to understand these features, we performed isolation, biochemical and enzymological characterization, molecular cloning and molecular modelling. The native enzyme is composed of two catalytic units (65 kDa each) and two propeptides (15 kDa each), yielding a molecular weight of 160 kDa
  • Fungal b-N-acetylhexosaminidases are inducible extracellular enzymes with many biotechnological applications. The enzyme from Penicillium oxalicum has unique enzymatic properties despite its close evolutionary relationship with other fungal hexosaminidases. It has high GalNAcase activity, tolerates substrates with the modified N-acyl group better and has some other unusual catalytic properties. In order to understand these features, we performed isolation, biochemical and enzymological characterization, molecular cloning and molecular modelling. The native enzyme is composed of two catalytic units (65 kDa each) and two propeptides (15 kDa each), yielding a molecular weight of 160 kDa (en)
Title
  • Enzymatic characterization and molecular modeling of an evolutionarily interesting fungal β-N-acetylhexosaminidase
  • Enzymatic characterization and molecular modeling of an evolutionarily interesting fungal β-N-acetylhexosaminidase (en)
skos:prefLabel
  • Enzymatic characterization and molecular modeling of an evolutionarily interesting fungal β-N-acetylhexosaminidase
  • Enzymatic characterization and molecular modeling of an evolutionarily interesting fungal β-N-acetylhexosaminidase (en)
skos:notation
  • RIV/67179843:_____/11:00366613!RIV12-AV0-67179843
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • P(1M0505), P(GA303/09/0477), P(GD305/09/H008), P(GP203/09/P024), P(LC06010), S, Z(AV0Z50200510), Z(AV0Z60870520), Z(MSM0021620808), Z(MSM6007665808)
http://linked.open...iv/cisloPeriodika
  • 14
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  • 197794
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  • RIV/67179843:_____/11:00366613
http://linked.open...riv/jazykVysledku
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  • deglycosylation; enzyme kinetics; hexosaminidase (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • GB - Spojené království Velké Británie a Severního Irska
http://linked.open...ontrolniKodProRIV
  • [FB0761E83D9D]
http://linked.open...i/riv/nazevZdroje
  • FEBS Journal
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  • 278
http://linked.open...iv/tvurceVysledku
  • Bezouška, Karel
  • Bojarová, Pavla
  • Ettrich, Rüdiger
  • Kulik, Natallia
  • Křen, Vladimír
  • Kumar, V.
  • Slámová, Kristýna
  • Vaněk, Ondřej
  • Doubnerová, V.
  • Kalendová, A.
  • Kukačka, Z.
  • Pompach, Petr
  • Ryšlavá, H.
  • Skočdopol, P.
http://linked.open...ain/vavai/riv/wos
  • 000292932700007
http://linked.open...n/vavai/riv/zamer
issn
  • 1742-464X
number of pages
http://bibframe.org/vocab/doi
  • 10.1111/j.1742-4658.2011.08173.x
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