Evidence map›Paper›PMID 30062637›Full record

ArticleMolecular biotechnology2018

Ig-like Domain in Endoglucanase Cel9A from Alicyclobacillus acidocaldarius Makes Dependent the Enzyme Stability on Calcium.

Mohammad Pazhang, Fereshteh S Younesi, Faramarz Mehrnejad, Saeed Najavand, Alireza Tarinejad, Mehrnaz Haghi, Fatemeh Rashno, Khosro Khajeh

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Article in Molecular biotechnology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

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3citing papers in PubMed
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3 · Its place in the literature

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3 citing papers in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

8 authors.

Mohammad PazhangDepartment of Cellular and Molecular Biology, Faculty of Science, Azarbaijan Shahid Madani University, Tabriz, Iran. pazhang@azaruniv.ac.ir.
Fereshteh S YounesiDepartment of Cellular and Molecular Biology, Faculty of Science, Azarbaijan Shahid Madani University, Tabriz, Iran.
Faramarz MehrnejadDepartment of Life Science Engineering, Faculty of New Sciences & Technologies, University of Tehran, Tehran, Iran.
Saeed NajavandDepartment of Cellular and Molecular Biology, Faculty of Science, Azarbaijan Shahid Madani University, Tabriz, Iran.
Alireza TarinejadDepartment of Biotechnology, Faculty of Agriculture, Azarbaijan Shahid Madani University, Tabriz, Iran.
Mehrnaz HaghiDepartment of Cellular and Molecular Biology, Faculty of Science, Azarbaijan Shahid Madani University, Tabriz, Iran.
Fatemeh RashnoDepartment of Biochemistry, Faculty of Biological Science, Tarbiat Modares University, Tehran, Iran.
Khosro KhajehDepartment of Biochemistry, Faculty of Biological Science, Tarbiat Modares University, Tehran, Iran.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Endoglucanase Cel9A from Alicyclobacillus acidocaldarius (AaCel9A) has an Ig-like domain and the enzyme stability is dependent to calcium. In this study the effect of calcium on the structure and stability of the wild-type enzyme and the truncated form (the wild-type enzyme without Ig-like domain, AaCel9AΔN) was investigated. Fluorescence quenching results indicated that calcium increased and decreased the rigidity of the wild-type and truncated enzymes, respectively. RMSF results indicated that AaCel9A has two flexible regions (regions A and B) and deleting the Ig-like domain increased the truncated enzyme stability by decreasing the flexibility of region B probably through increasing the hydrogen bonds. Calcium contact map analysis showed that deleting the Ig-like domain decreased the calcium contacting residues and their calcium binding affinities, especially, in region B which has a role in calcium binding site in AaCel9A. Metal depletion and activity recovering as well as stability results showed that the structure and stability of the wild-type and truncated enzymes are completely dependent on and independent of calcium, respectively. Finally, one can conclude that the deletion of Ig-like domain makes AaCel9AΔN independent of calcium via decreasing the flexibility of region B through increasing the hydrogen bonds. This suggests a new role for the Ig-like domain which makes AaCel9A structure dependent on calcium.

Indexed as

AlicyclobacillusBinding SitesCalciumCellulaseEnzyme StabilityImmunoglobulin DomainsProtein BindingSubstrate SpecificityCalciumCellulaseCalciumEndoglucanase Cel9AIg-like domainMolecular dynamics simulation

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.