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contributor authorمحمدرضا حسین دختen
contributor authorMohammad Reza Bozorgmehren
contributor authorحسین اشتیاق حسینیen
contributor authorراضیه جلالen
contributor authorاحمد آسودهen
contributor authorMahin Saberien
contributor authorZeinab Haratipouren
contributor authorحسن منهمیen
contributor authorMohammad Reza Housaindokhtfa
contributor authorHossein Eshtiagh Hosseinifa
contributor authorRazieh Jalalfa
contributor authorAhmad Asoodehfa
contributor authorHassan Monhemifa
date accessioned2020-06-06T13:12:58Z
date available2020-06-06T13:12:58Z
date issued2013
identifier urihttps://libsearch.um.ac.ir:443/fum/handle/fum/3346209?locale-attribute=fa&show=full
description abstractIn this work, structures of the native (Amyl-C) and truncated Taka amylase were compared by

molecular modeling methods. Using in silico enzyme engineering approach, 50 (Amyl-S1) and

100 (Amyl-S2) amino acids were eliminated from Amyl-C to produce the truncated forms.

Analysis of the tertiary structures showed that three essential domains of the enzyme including

super 8 , the barrel region, and the large cleft remained native in Amyl-

S1 and Amyl-S2. Secondary structures of Met112-Val118, Gly202-His211, Gln230-Asp233,

Phe292-Asp297 residues in Amyl-C, Amyl-S1, and Amyl-S2 remained unchanged. These

domains are necessary for catalytic function of alpha-amylase superfamily. Flexibility analysis of

the three forms was examined and it is obtained that by truncation, the flexibility of the Cterminal

domain was increased. This shows that C-terminal domain is essential for the stability

of the structure which is in agreement with experimental observations. However, Glu156, Gln

162, Gly234, Val 245, Asn260, Ser264, Asp 297 of Amyl-C had higher flexibility than those in

truncated enzymes. Maltoriose, Maltotetraose, Maltopentaose, Maltohexaose and maltoheptaose

as five substrates were docked to the three enzyme forms. Binding affinity of maltoheptaose was

higher in Amyl-C and Amyl-S1and lower in Amyl-S2 than that of Maltoriose. In all forms the

substrates were associated with three residues of the catalytic triad.
en
languageEnglish
titleStructural properties of the truncated and wild types of Taka-amylase: A molecular dynamics simulation and docking studyen
typeJournal Paper
contenttypeExternal Fulltext
subject keywordsprotein engineeringen
subject keywordstruncated amylaseen
subject keywordsGromacsen
subject keywordsC-terminalen
journal titleJournal of Molecular Catalysis B: Enzymaticfa
pages36-40
journal volume95
journal issue0
identifier linkhttps://profdoc.um.ac.ir/paper-abstract-1034702.html
identifier articleid1034702


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