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Enzymes02:34

Enzymes

Inside living organisms, enzymes act as catalysts for many biochemical reactions involved in cellular metabolism. The role of enzymes is to reduce the activation energies of biochemical reactions by forming complexes with its substrates. The lowering of activation energies favor an increase in the rates of biochemical reactions.
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...
Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes a mild...
Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes a mild...
Introduction to Enzymes01:22

Introduction to Enzymes

The use of enzymes by humans dates to 7000 BCE. Humans first used enzymes to ferment sugars and produce alcohol without knowing that this was an enzyme-catalyzed reaction. Wilhelm Kuhne coined the term 'enzyme' in 1877 from the Greek words ‘en’ meaning ‘in’ or ‘within’ and ‘zyme’ meaning ‘yeast.’
Most enzymes are proteins that speed up biochemical reactions without being consumed. Enzymes contain one or more active sites that bind the substrates and convert them into products. Many enzymes also...
Introduction To Enzymes01:22

Introduction To Enzymes

The use of enzymes by humans dates to 7000 BCE. Humans first used enzymes to ferment sugars and produce alcohol without knowing that this was an enzyme-catalyzed reaction. Wilhelm Kuhne coined the term 'enzyme' in 1877 from the Greek words ‘en’ meaning ‘in’ or ‘within’ and ‘zyme’ meaning ‘yeast.’
Most enzymes are proteins that speed up biochemical reactions without being consumed. Enzymes contain one or more active sites that bind the substrates and convert them into products. Many enzymes also...
Catalytically Perfect Enzymes01:07

Catalytically Perfect Enzymes

The theory of catalytically perfect enzymes was first proposed by W.J. Albery and J. R. Knowles in 1976. These enzymes catalyze biochemical reactions at high-speed. Their catalytic efficiency values range from 108-109 M-1s-1. These enzymes are also called 'diffusion-controlled' as the only rate-limiting step in the catalysis is that of the substrate diffusion into the active site. Examples include triose phosphate isomerase, fumarase, and superoxide dismutase.

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Updated: May 21, 2026

Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions
13:00

Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions

Published on: April 4, 2014

Los colgajos ampliamente abiertos son clave para la actividad de la ureasa.

Benjamin P Roberts1, Bill R Miller, Adrian E Roitberg

  • 1Quantum Theory Project, University of Florida, P.O. Box 118435, Gainesville, Florida 32611-8435, USA.

Journal of the American Chemical Society
|June 8, 2012
PubMed
Resumen

Los investigadores descubrieron un nuevo estado abierto de la capa de la enzima ureasa. Este hallazgo revela más del sitio activo, ofreciendo nuevas posibilidades para el descubrimiento de fármacos dirigidos a la ureasa.

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Área de la Ciencia:

  • La bioquímica es la bioquímica.
  • Enzimología Enzimología.
  • Biología Estructural Biología estructural.

Sus antecedentes:

  • La actividad de la enzima ureasa está regulada por un colgajo en el sitio activo que controla el movimiento del sustrato y del producto.
  • Comprender la dinámica conformacional de la ureasa es crucial para la inhibición enzimática y el desarrollo de fármacos.

Objetivo del estudio:

  • Para investigar los estados conformacionales del colgajo del sitio activo de la ureasa utilizando simulaciones de dinámica molecular.
  • Identificar nuevos estados del colgajo del sitio activo de la ureasa que podrían ser explotados para el descubrimiento de fármacos.

Principales métodos:

  • Se utilizaron simulaciones de dinámica molecular (DM) para explorar el paisaje conformacional de la solapa del sitio activo de la ureasa.
  • Se analizaron las trayectorias de simulación para identificar distintos estados de colgajo y sus barreras de energía asociadas.

Principales resultados:

  • Se identificó un estado de flap de ureasa ampliamente abierto y no observado previamente, distinto de los estados cerrados y abiertos conocidos.
  • Se demostró que el estado abierto proporciona un acceso fácil al grupo metálico del sitio activo de la ureasa.
  • Se observó una región expuesta al disolvente en el bolsillo de unión incluso cuando el colgajo está cerrado, lo que sugiere un potencial reservorio de sustrato / producto.

Conclusiones:

  • El estado de colgajo ampliamente abierto recientemente identificado expande significativamente el bolsillo accesible del sitio activo de la ureasa.
  • Esta bolsa expandida presenta nuevas oportunidades para diseñar inhibidores de moléculas pequeñas y fármacos dirigidos a la ureasa.
  • El potencial reservorio de sustrato/producto justifica una mayor investigación de su papel en la función enzimática.