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Keywords: enzyme catalysis
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Articles

Metal-induced change in catalytic loop positioning in Helicobacter pylori arginase alters catalytic function

Ankita Dutta, Mohit Mazumder, Mashkoor Alam, Samudrala Gourinath, Apurba Kumar Sau
Journal: Biochemical Journal
Biochem J (2019) 476 (23): 3595–3614.
https://doi.org/10.1042/BCJ20190545
Published: 10 December 2019
... ( apurbaksau@gmail.com , apurba@nii.res.in ) 28 7 2019 14 11 2019 18 11 2019 20 11 2019 © 2019 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society 2019 enzyme catalysis fluorescence anisotropy decays molecular dynamics simulations...
View article titled, Metal-induced change in catalytic loop positioning in Helicobacter pylori arginase alters catalytic function
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Includes: Supplementary data
Articles

Identification of active site residues implies a two-step catalytic mechanism for acyl-ACP thioesterase

Fuyuan Jing, Marna D. Yandeau-Nelson, Basil J. Nikolau
Journal: Biochemical Journal
Biochem J (2018) 475 (23): 3861–3873.
https://doi.org/10.1042/BCJ20180470
Published: 10 December 2018
... ) or Marna D. Yandeau-Nelson ( myn@iastate.edu ) 17 6 2018 6 11 2018 7 11 2018 8 11 2018 © 2018 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society 2018 acyl-ACP thioesterase enzyme catalysis enzyme mechanism fatty acid synthase site...
View article titled, Identification of active site residues implies a two-step catalytic mechanism for acyl-ACP thioesterase
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Includes: Supplementary data
Articles

Directed evolution of Tau class glutathione transferases reveals a site that regulates catalytic efficiency and masks co-operativity

Irine Axarli, Abdi W. Muleta, Dimitrios Vlachakis, Sophia Kossida, Georgia Kotzia, Anastasios Maltezos, Prathusha Dhavala, Anastassios C. Papageorgiou, Nikolaos E. Labrou
Journal: Biochemical Journal
Biochem J (2016) 473 (5): 559–570.
https://doi.org/10.1042/BJ20150930
Published: 24 February 2016
... shuffling showed allosteric kinetics and enhanced detoxifying potential towards the herbicide fluorodifen. Its structure was determined. New engineered GSTs could be useful in biotechnology as efficient bioscavengers. allosteric regulation enzyme catalysis enzyme kinetics enzyme structure...
View article titled, Directed evolution of Tau class glutathione transferases reveals a site that regulates catalytic efficiency and masks co-operativity
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Includes: Supplementary data
Articles

Structures of lipoyl synthase reveal a compact active site for controlling sequential sulfur insertion reactions

Jenny E. Harmer, Martyn J. Hiscox, Pedro C. Dinis, Stephen J. Fox, Andreas Iliopoulos, James E. Hussey, James Sandy, Florian T. Van Beek, Jonathan W. Essex, Peter L. Roach
Journal: Biochemical Journal
Biochem J (2014) 464 (1): 123–133.
https://doi.org/10.1042/BJ20140895
Published: 23 October 2014
... Journal compilation © 2014 Biochemical Society 2014 cofactor crystal structure enzyme catalysis lipoyl synthase radical S -adenosylmethionine (SAM) sulfur Thermosynechococcus elongatus 1 These authors are joint first authors for this paper. 2 To whom correspondence...
View article titled, Structures of lipoyl synthase reveal a compact active site for controlling sequential sulfur insertion reactions
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Articles

The Glu 216 /Ser 218 pocket is a major determinant of spermine oxidase substrate specificity

Manuela Cervelli, Emanuela Angelucci, Pasquale Stano, Loris Leboffe, Rodolfo Federico, Giovanni Antonini, Paolo Mariottini, Fabio Polticelli
Journal: Biochemical Journal
Biochem J (2014) 461 (3): 453–459.
https://doi.org/10.1042/BJ20140305
Published: 10 July 2014
... endows spermine oxidase with acetylpolyamine oxidase activity. Glu 216 and Ser 218 are major determinants of spermine oxidase substrate specificity. This finding will allow for the design of specific inhibitors for these enzymes. acetylpolyamine oxidase (APAO) enzyme catalysis enzyme kinetics...
View article titled, The Glu 216 /Ser 218 pocket is a major determinant of spermine oxidase substrate specificity
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Articles

A dual conformation of the post-decarboxylation intermediate is associated with distinct enzyme states in mycobacterial KGD (α-ketoglutarate decarboxylase)

Tristan Wagner, Nathalie Barilone, Pedro M. Alzari, Marco Bellinzoni
Journal: Biochemical Journal
Biochem J (2014) 457 (3): 425–434.
https://doi.org/10.1042/BJ20131142
Published: 10 January 2014
... of mycobacterial KGD revealed two post-decarboxylation intermediate conformations and concerted large-scale motions along the catalytic cycle, which may exemplify a trait of E1o enzymes. bacterial metabolism decarboxylase dehydrogenase enzyme catalysis Mycobacterium protein dynamics X-ray...
View article titled, A dual conformation of the post-decarboxylation intermediate is associated with distinct enzyme states in mycobacterial KGD (α-ketoglutarate decarboxylase)
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Includes: Supplementary data
Articles

Molecular recognition of physiological substrate noradrenaline by the adrenaline-synthesizing enzyme PNMT and factors influencing its methyltransferase activity

Nyssa Drinkwater, Christine L. Gee, Munish Puri, Kevin R. Criscione, Michael J. McLeish, Gary L. Grunewald, Jennifer L. Martin
Journal: Biochemical Journal
Biochem J (2009) 422 (3): 463–471.
https://doi.org/10.1042/BJ20090702
Published: 27 August 2009
...Nyssa Drinkwater; Christine L. Gee; Munish Puri; Kevin R. Criscione; Michael J. McLeish; Gary L. Grunewald; Jennifer L. Martin Substrate specificity is critically important for enzyme catalysis. In the adrenaline-synthesizing enzyme PNMT (phenylethanolamine N -methyltransferase), minor changes...
View article titled, Molecular recognition of physiological substrate noradrenaline by the adrenaline-synthesizing enzyme PNMT and factors influencing its methyltransferase activity
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Includes: Supplementary data
Articles

A functionally conserved basic residue in glutathione transferases interacts with the glycine moiety of glutathione and is pivotal for enzyme catalysis

Ardcharaporn Vararattanavech, Albert J. Ketterman
Journal: Biochemical Journal
Biochem J (2007) 406 (2): 247–256.
https://doi.org/10.1042/BJ20070422
Published: 13 August 2007
... network. In the GSTD (Delta class GST) studied, adGSTD4-4, the network consisted of His 38 , Met 39 , Asn 47 , Gln 49 , His 50 and Cys 51 . In addition to contributing to glutathione binding, this region also had major effects on enzyme catalysis, as shown by changes in kinetic parameters and substrate...
View article titled, A functionally conserved basic residue in glutathione transferases interacts with the glycine moiety of glutathione and is pivotal for <span class="search-highlight">enzyme</span> <span class="search-highlight">catalysis</span>
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Articles

Catalytic mechanism of the glutathione peroxidase-type tryparedoxin peroxidase of Trypanosoma brucei

Tanja Schlecker, Marcelo A. Comini, Johannes Melchers, Thomas Ruppert, R. Luise Krauth-Siegel
Journal: Biochemical Journal
Biochem J (2007) 405 (3): 445–454.
https://doi.org/10.1042/BJ20070259
Published: 13 July 2007
... that of the selenoenzymes. © The Authors Journal compilation © 2007 Biochemical Society 2007 1 To whom correspondence should be addressed (email luise.krauth-siegel@bzh.uni-heidelberg.de ). 19 2 2007 13 4 2007 25 4 2007 25 4 2007 enzyme catalysis glutathione peroxidase-type...
View article titled, Catalytic mechanism of the glutathione peroxidase-type tryparedoxin peroxidase of Trypanosoma brucei
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Articles

Models for enzyme superactivity in aqueous solutions of surfactants

Paolo VIPARELLI, Francesco ALFANI, Maria CANTARELLA
Journal: Biochemical Journal
Biochem J (1999) 344 (3): 765–773.
https://doi.org/10.1042/bj3440765
Published: 08 December 1999
...-shaped dependence on surfactant concentration. The effect of the partition of enzyme and substrate is described, as is that of enzyme efficiency in the various pseudo-phases. Key words: enzyme catalysis, kinetics models, micelles. ammonium bromide (CTBABr) and cetyltripropylammonium bromide gave the most...
View article titled, Models for enzyme superactivity in aqueous solutions of surfactants
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