Repo Dosen ULM

Tyr320 is a molecular determinant of the catalytic activity of β-glucosidase from Neosartorya fischeri.

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dc.contributor.author Shanmugam, Ramasamy
dc.contributor.author Kim, In-Won
dc.contributor.author Tiwari, Manish K.
dc.contributor.author Hui, Gao
dc.contributor.author Mardina, Primata
dc.contributor.author Das, Devashish
dc.contributor.author Kumar, Anurag
dc.contributor.author Jeya, Marimuthu
dc.contributor.author Kim, sang
dc.contributor.author Kim, Young Sin
dc.contributor.author Lee, Jung-Kul
dc.date.accessioned 2022-07-28T01:07:55Z
dc.date.available 2022-07-28T01:07:55Z
dc.date.issued 2020-05
dc.identifier.issn 0141-8130
dc.identifier.uri https://repo-dosen.ulm.ac.id//handle/123456789/24932
dc.description.abstract β-Glucosidases (BGL) are key members of the cellulase enzyme complex that determine efficiency of lignocellu losic biomass degradation, which have shown great functional importance to many biotechnological systems. A previous reported BGL from Neosartorya fischeri (NfBGL) showed much higher activity than other BGLs. Screening the important residues based on sequence alignment, analyzing a homology model, and subsequent alteration of individually screened residues by site-directed mutagenesis were carried out to investigate the molecular deter minants of the enzyme's high catalytic efficiency. Tyr320, located in the wild-type NfBGL substrate-binding pocket was identified as crucial to the catalytic function of NfBGL. The replacement of Tyr320 with aromatic amino acids did not significantly alter the catalytic efficiency towards p-nitrophenyl β-D-glucopyranoside (pNPG). However, mutants with charged and hydrophilic amino acids showed almost no activity towards pNPG. Computational studies suggested that an aromatic acid is required at position 320 in NfBGL to stabilize the enzyme-substrate complex formation. This knowledge on the mechanism of action of the molecular determi nants can also help rational protein engineering of BGLs. en_US
dc.language.iso en en_US
dc.publisher Elsevier en_US
dc.subject Catalytic efficiency en_US
dc.subject b-Glucosidase en_US
dc.subject Substrate affinity en_US
dc.subject phi-Sigma interaction en_US
dc.subject MD simulation en_US
dc.title Tyr320 is a molecular determinant of the catalytic activity of β-glucosidase from Neosartorya fischeri. en_US
dc.type Other en_US


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