Source: International journal of molecular sciences [Int J Mol Sci] 2024 Nov 24; Vol. 25 (23). Date of Electronic Publication: 2024 Nov 24.Publisher: MDPI Country of Publication: Switzerland NLM ID: 101092791 Publication Model: Electronic Cited Medium: Internet ISSN: 1422-0067

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Academic Journal

The Trajectory of Damaged-Base Eversion into the Active Site of Apurinic/Apyrimidinic Endonuclease APE1 Regulates This Enzyme's Substrate Specificity.

Authors : Bulygin AA; Institute of Chemical Biology and Fundamental Medicine, Siberian Branch of Russian Academy of Sciences, Novosibirsk 630090, Russia.; Kuznetsov NA

Subjects: DNA-(Apurinic or Apyrimidinic Site) Lyase*/DNA-(Apurinic or Apyrimidinic Site) Lyase*/DNA-(Apurinic or Apyrimidinic Site) Lyase*/metabolism ; DNA-(Apurinic or Apyrimidinic Site) Lyase*/DNA-(Apurinic or Apyrimidinic Site) Lyase*/DNA-(Apurinic or Apyrimidinic Site) Lyase*/chemistry ; Catalytic Domain*

Source: International journal of molecular sciences [Int J Mol Sci] 2024 Nov 15; Vol. 25 (22). Date of Electronic Publication: 2024 Nov 15.Publisher: MDPI Country of Publication: Switzerland NLM ID: 101092791 Publication Model: Electronic Cited Medium: Internet ISSN: 1422-0067

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Elucidating the Substrate Envelope of Enterovirus 68-3C Protease: Structural Basis of Specificity and Potential Resistance.

Authors : Azzolino VN; Department of Biochemistry and Molecular Biotechnology, University of Massachusetts Chan Medical School, Worcester, MA 01605, USA.; Shaqra AM

Subjects: 3C Viral Proteases*/3C Viral Proteases*/3C Viral Proteases*/chemistry ; 3C Viral Proteases*/3C Viral Proteases*/3C Viral Proteases*/metabolism ; Molecular Dynamics Simulation*

Source: Viruses [Viruses] 2024 Sep 05; Vol. 16 (9). Date of Electronic Publication: 2024 Sep 05.Publisher: MDPI Country of Publication: Switzerland NLM ID: 101509722 Publication Model: Electronic Cited Medium: Internet ISSN: 1999-4915

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Computational studies on the catalytic potential of the double active site for enzyme engineering.

Authors : Krishna NB; Department of Computational Biology and AI, Kcat Enzymatic Private Limited, #16, Ramakrishnappa Road, Cox Town, Bangalore, 560005, India.; Department of Biotechnology and Bioinformatics, JSS Academy of Higher Education and Research, Mysuru, 570015, India.

Subjects: Catalytic Domain* ; Molecular Dynamics Simulation* ; Protein Engineering*/Protein Engineering*/Protein Engineering*/methods

Source: Scientific reports [Sci Rep] 2024 Aug 02; Vol. 14 (1), pp. 17892. Date of Electronic Publication: 2024 Aug 02.Publisher: Nature Publishing Group Country of Publication: England NLM ID: 101563288 Publication Model: Electronic Cited Medium: Internet ISSN:

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In silico approaches to study the human asparagine synthetase: An insight of the interaction between the enzyme active sites and its substrates.

Authors : Riaz A; Department of Biotechnology, Lahore College for Women University, Lahore, Pakistan.; Kaleem A

Subjects: Aspartate-Ammonia Ligase*/Aspartate-Ammonia Ligase*/Aspartate-Ammonia Ligase*/metabolism ; Aspartate-Ammonia Ligase*/Aspartate-Ammonia Ligase*/Aspartate-Ammonia Ligase*/chemistry ; Aspartate-Ammonia Ligase*/Aspartate-Ammonia Ligase*/Aspartate-Ammonia Ligase*/genetics

Source: PloS one [PLoS One] 2024 Aug 02; Vol. 19 (8), pp. e0307448. Date of Electronic Publication: 2024 Aug 02 (Print Publication: 2024).Publisher: Public Library of Science Country of Publication: United States NLM ID: 101285081 Publication Model: eCollection Cited Medium: Internet

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Academic Journal

Structural determinants of cold activity and glucose tolerance of a family 1 glycoside hydrolase (GH1) from Antarctic Marinomonas sp. ef1.

Authors : Gourlay LJ; Department of Biosciences, University of Milano, Italy.; Mangiagalli M

Subjects: Cold Temperature* ; Marinomonas*/Marinomonas*/Marinomonas*/enzymology ; Marinomonas*/Marinomonas*/Marinomonas*/genetics

Source: The FEBS journal [FEBS J] 2024 Jul; Vol. 291 (13), pp. 2897-2917. Date of Electronic Publication: 2024 Feb 23.Publisher: Published by Blackwell Pub. on behalf of the Federation of European Biochemical Societies Country of Publication: England NLM ID: 101229646 Publication

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Substrate Activation Efficiency in Active Sites of Hydrolases Determined by QM/MM Molecular Dynamics and Neural Networks.

Authors : Polyakov IV; Chemistry Department, Lomonosov Moscow State University, 119991 Moscow, Russia.; Meteleshko YI

Subjects: Neural Networks, Computer* ; Molecular Dynamics Simulation* ; Hydrolases*/Hydrolases*/Hydrolases*/chemistry

Source: International journal of molecular sciences [Int J Mol Sci] 2025 May 26; Vol. 26 (11). Date of Electronic Publication: 2025 May 26.Publisher: MDPI Country of Publication: Switzerland NLM ID: 101092791 Publication Model: Electronic Cited Medium: Internet ISSN: 1422-0067

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Impact of Phosphorylation at Various Sites on the Active Pocket of Human Ferrochelatase: Insights from Molecular Dynamics Simulations.

Authors : Guo M; School of Chemistry, IGCME, Sun Yat-sen University, Guangzhou 510006, China.; Lin Y

Subjects: Ferrochelatase*/Ferrochelatase*/Ferrochelatase*/metabolism ; Ferrochelatase*/Ferrochelatase*/Ferrochelatase*/chemistry ; Molecular Dynamics Simulation*

Source: International journal of molecular sciences [Int J Mol Sci] 2024 Jun 08; Vol. 25 (12). Date of Electronic Publication: 2024 Jun 08.Publisher: MDPI Country of Publication: Switzerland NLM ID: 101092791 Publication Model: Electronic Cited Medium: Internet ISSN: 1422-0067

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A salt bridge of the C-terminal carboxyl group regulates PHPT1 substrate affinity and catalytic activity.

Authors : Zavala E; Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut, USA.; Dansereau S

Subjects: Catalytic Domain* ; Molecular Dynamics Simulation*; Humans

Source: Protein science : a publication of the Protein Society [Protein Sci] 2024 Jun; Vol. 33 (6), pp. e5009.Publisher: Cold Spring Harbor Laboratory Press Country of Publication: United States NLM ID: 9211750 Publication Model: Print Cited Medium: Internet

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Molecular dynamics, docking and quantum calculations reveal conformational changes influenced by CYP271A amino acid mutations related to cerebrotendinous xanthomatosis.

Authors : Sixto-López Y; Departamento de Química Farmacéutica y Orgánica, Facultad de Farmacia, Universidad de Granada, Campus de Cartuja s/n, 18071, Granada, Spain. .; Laboratorio de Diseño y Desarrollo de Nuevos Fármacos e Innovación Biotecnológica (Laboratory for the Design and Development of New Drugs and Biotechnological Innovation), Escuela Superior de Medicina, Plan de San Luis y Díaz Mirón, Instituto Politécnico Nacional, Ciudad de México, 11340, México. .

Subjects: Xanthomatosis, Cerebrotendinous*/Xanthomatosis, Cerebrotendinous*/Xanthomatosis, Cerebrotendinous*/genetics ; Cholestanetriol 26-Monooxygenase*/Cholestanetriol 26-Monooxygenase*/Cholestanetriol 26-Monooxygenase*/genetics ; Cholestanetriol 26-Monooxygenase*/Cholestanetriol 26-Monooxygenase*/Cholestanetriol 26-Monooxygenase*/chemistry

Source: Scientific reports [Sci Rep] 2025 Mar 25; Vol. 15 (1), pp. 10229. Date of Electronic Publication: 2025 Mar 25.Publisher: Nature Publishing Group Country of Publication: England NLM ID: 101563288 Publication Model: Electronic Cited Medium: Internet ISSN:

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نتائج البحث

فلترة النتائج

Conformational Flexibility of the C-Terminal Region Influences Distal Active Site Residues Across the Tautomerase Superfamily.

The Trajectory of Damaged-Base Eversion into the Active Site of Apurinic/Apyrimidinic Endonuclease APE1 Regulates This Enzyme's Substrate Specificity.

Elucidating the Substrate Envelope of Enterovirus 68-3C Protease: Structural Basis of Specificity and Potential Resistance.

Computational studies on the catalytic potential of the double active site for enzyme engineering.

In silico approaches to study the human asparagine synthetase: An insight of the interaction between the enzyme active sites and its substrates.

Structural determinants of cold activity and glucose tolerance of a family 1 glycoside hydrolase (GH1) from Antarctic Marinomonas sp. ef1.

Substrate Activation Efficiency in Active Sites of Hydrolases Determined by QM/MM Molecular Dynamics and Neural Networks.

Impact of Phosphorylation at Various Sites on the Active Pocket of Human Ferrochelatase: Insights from Molecular Dynamics Simulations.

A salt bridge of the C-terminal carboxyl group regulates PHPT1 substrate affinity and catalytic activity.

Molecular dynamics, docking and quantum calculations reveal conformational changes influenced by CYP271A amino acid mutations related to cerebrotendinous xanthomatosis.

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