Dynamic Connection between Enzymatic Catalysis and Collective Protein Motions

Human porphobilinogen synthase (PBGS) can exist in two dramatically different quaternary structure isoforms, which have been proposed to be in dynamic equilibrium (Breinig, S., Kervinen, J., Stith, L., Wasson, A. S., Fairman, R., Wlodawer, A., Zdanov, A., and Jaffe, E. K. (2003)Nat. Struct. Biol.10, 757–763). The quaternary structure isoforms of PBGS result from two alternative conformations of the monomer; one monomer structure assembles into a high activity octamer, whereas the other monomer structure assembles into a low activity hexamer. The kinetic behavior of these oligomers led to the hypothesis that turnover facilitates the interconversion of the oligomeric structures. The current work demonstrates that the interactions of ligands at the enzyme active site promote the structural interconversion between human PBGS quaternary structure isoforms, favoring formation of the octamer. This observation illustrates that the assembly and disassembly of oligomeric proteins can be facilitated by the protein motions that accompany enzymatic catalysis.

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Linking Electrostatic Effects and Protein Motions in Enzymatic Catalysis. A Theoretical Analysis of CatecholO-Methyltransferase

The Journal of Physical Chemistry B ◽

10.1021/jp505746x ◽

2014 ◽

Vol 119 (3) ◽

pp. 873-882 ◽

Cited By ~ 11

Author(s):

Rafael García-Meseguer ◽

Kirill Zinovjev ◽

Maite Roca ◽

Javier J. Ruiz-Pernía ◽

Iñaki Tuñón

Keyword(s):

Theoretical Analysis ◽

Enzymatic Catalysis ◽

Electrostatic Effects ◽

Protein Motions

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Matrix metalloproteinases: structure, functions and genetic polymorphism

Nauchno-prakticheskii zhurnal «Patogenez» ◽

10.25557/gm.2017.2.7297 ◽

2017 ◽

pp. 14-23

Author(s):

А.С. Шадрина ◽

И.В. Терешкина ◽

Я.З. Плиева ◽

Д.Н. Кушлинский ◽

Д.О. Уткин ◽

...

Keyword(s):

Genetic Polymorphism ◽

Matrix Metalloproteinases ◽

Active Center ◽

Human Body ◽

Enzymatic Catalysis ◽

Structure Functions ◽

Zinc Ion ◽

Etiological Factors ◽

Mmp Genes

Матриксные металлопротеиназы (ММП) - ферменты класса гидролаз, осуществляющие ферментативный катализ с помощью связанного в активном центре иона цинка. Функции ММП разнообразны, и нарушение баланса их активности может быть одним из этиологических факторов различных заболеваний. В данном обзоре рассмотрена классификация ММП человека, особенности их структуры и регуляции, а также роль в физиологических и патологических процессах в организме человека. Приведен перечень наиболее изученных на настоящий момент полиморфных вариантов генов MMП, описаны их функциональные эффекты и представлены результаты ассоциативных исследований. Matrix metalloproteinases (MMPs) are enzymes of the hydrolase class that carry out enzymatic catalysis with the help of a zinc ion bound in the active center. MMP functions are diverse, and a disturbance in the balance of their activity may be one of the etiological factors of various diseases. In this review, the classification of human MMP, the features of their structure and regulation, as well as the role in physiological and pathological processes in the human body are considered. A list of the most studied polymorphic versions of MMP genes has been given, their functional effects have been described, and the results of associative studies have been presented.

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Identification of the reactive cysteines of Escherichia coli 5-enolpyruvylshikimate-3-phosphate synthase and their nonessentiality for enzymatic catalysis.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)77947-2 ◽

1988 ◽

Vol 263 (4) ◽

pp. 1798-1802

Author(s):

S R Padgette ◽

Q K Huynh ◽

S Aykent ◽

R D Sammons ◽

J A Sikorski ◽

...

Keyword(s):

Escherichia Coli ◽

Enzymatic Catalysis ◽

Phosphate Synthase

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The Role of Hydrophobicity in Supramolecular Polymer/Surfactant Catalysts: An Understandable Model for Enzymatic Catalysis

Journal of Colloid and Interface Science ◽

10.1016/j.jcis.2020.12.081 ◽

2020 ◽

Author(s):

Paulo F.A. Costa ◽

Rafael de Abreu ◽

Andressa B. Fontana ◽

Haidi D. Fiedler ◽

Anthony J. Kirby ◽

...

Keyword(s):

Enzymatic Catalysis ◽

Supramolecular Polymer ◽

Polymer Surfactant

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Sampling Long Time Scale Protein Motions: OSRW Simulation of Active Site Loop Conformational Free Energies in Formyl-CoA:Oxalate CoA Transferase

Journal of the American Chemical Society ◽

10.1021/ja101446u ◽

2010 ◽

Vol 132 (21) ◽

pp. 7252-7253 ◽

Cited By ~ 8

Author(s):

Sangbae Lee ◽

Mengen Chen ◽

Wei Yang ◽

Nigel G. J. Richards

Keyword(s):

Active Site ◽

Time Scale ◽

Free Energies ◽

Protein Motions ◽

Coa Transferase ◽

Long Time

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Development of a new amperometric biosensor based on polyphenoloxidase and polyethersulphone membrane

Pure and Applied Chemistry ◽

10.1351/pac200173121993 ◽

2001 ◽

Vol 73 (12) ◽

pp. 1993-1999 ◽

Cited By ~ 10

Author(s):

P. V. Climent ◽

M. L. M. Serralheiro ◽

M. J. F. Rebelo

Keyword(s):

Phenolic Compounds ◽

Response Time ◽

Enzyme Immobilization ◽

Platinum Electrode ◽

Enzymatic Catalysis ◽

Amperometric Biosensor ◽

Catecholase Activity

An amperometric biosensor based on the enzyme polyphenoloxidase (PPO), which makes the bioelectrocatalysis of phenolic compounds, was developed and optimized using cathecol as substrate. Polyethersulphone membranes were used for enzyme immobilization. Polyphenoloxidase oxidizes monophenols (cresolase activity) and diphenols (catecholase activity) into the corresponding o-quinones; the o-quinones formed in the enzymatic catalysis are then reduced back to cathecol at 200 mV (vs. Ag, AgCl) at a platinum electrode. The polyphenoloxidase immobilized was from commercial origin or extracted from mushrooms. p-Cresol and phenol substrates were also tested. Reproducibility, response time, linearity, sensitivity, and stability of the biosensor were studied.

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