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Related Concept Videos

Pharmacogenetics of Phase I Enzymes: Cytochrome P450 Isozymes01:28

Pharmacogenetics of Phase I Enzymes: Cytochrome P450 Isozymes

Cytochrome P450 (CYP450) enzymes are a superfamily of heme-containing monooxygenases that play a pivotal role in Phase I drug metabolism by catalyzing oxidation and reduction reactions.These enzymes transform lipophilic xenobiotics into more hydrophilic metabolites, facilitating subsequent Phase II conjugation and eventual excretion. The CYP450 family is classified into families (e.g., CYP1–CYP3) and subfamilies (e.g., CYP2A, CYP2C), based on amino acid sequence homology.CYP450 isoenzymes,...
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.
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

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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...
Drug Metabolism: Phase I Reactions01:17

Drug Metabolism: Phase I Reactions

A phase I reaction is a biochemical process that introduces a functionally reactive polar group to a substance. This transformation predominantly occurs in the liver, facilitated by the cytochrome P450 system of hemoproteins situated in the lipophilic endoplasmic reticulum of cells. The metabolite generated through this process can have varying polarities. If it is sufficiently polar, it can be easily excreted in the urine due to its water compatibility. However, if the metabolite is nonpolar,...
Enzyme Kinetics01:19

Enzyme Kinetics

Enzymes speed up reactions by lowering the activation energy of the reactants. The speed at which the enzyme turns reactants into products is called the rate of reaction. Several factors impact the rate of reaction, including the number of available reactants. Enzyme kinetics is the study of how an enzyme changes the rate of a reaction.
Scientists typically study enzyme kinetics with a fixed amount of enzyme in the controlled environment of a test tube. When more reactant, or substrate, is...

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Formation of Covalent DNA Adducts by Enzymatically Activated Carcinogens and Drugs In Vitro and Their Determination by 32P-postlabeling
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Formation of Covalent DNA Adducts by Enzymatically Activated Carcinogens and Drugs In Vitro and Their Determination by 32P-postlabeling

Published on: March 20, 2018

Cytochrome P450: taming a wild type enzyme.

Sang Taek Jung1, Ryan Lauchli, Frances H Arnold

  • 1Divison of Chemistry and Chemical Engineering 210-41, California Institute of Technology, Pasadena, CA 91125, USA.

Current Opinion in Biotechnology
|March 18, 2011
PubMed
Summary

Protein engineering of cytochrome P450 monooxygenases (P450s) has yielded novel catalytic functions for synthesizing drug metabolites and natural products. These enzymes are highly evolvable, readily adapting to new substrates and selectivities through mutation.

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Synthesis of Protein Bioconjugates via Cysteine-maleimide Chemistry
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Formation of Covalent DNA Adducts by Enzymatically Activated Carcinogens and Drugs In Vitro and Their Determination by 32P-postlabeling

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Synthesis of Protein Bioconjugates via Cysteine-maleimide Chemistry
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Synthesis of Protein Bioconjugates via Cysteine-maleimide Chemistry

Published on: July 20, 2016

Area of Science:

  • Biocatalysis
  • Enzyme Engineering
  • Synthetic Biology

Background:

  • Cytochrome P450 monooxygenases (P450s) are versatile enzymes with significant applications in chemical synthesis.
  • Protein engineering has successfully created P450s with non-natural activities for synthesizing drug metabolites and precursors for artemisinin and paclitaxel.
  • P450s exhibit remarkable robustness and adaptability to mutations within their active sites, suggesting high evolvability.

Purpose of the Study:

  • To highlight the successful protein engineering of P450s for novel applications.
  • To discuss the inherent evolvability of P450 enzymes.
  • To explore the structural basis for P450s' adaptability.

Main Methods:

  • Literature review of protein engineering studies on P450s.
  • Analysis of P450 active site properties and conformational flexibility.
  • Case studies on P450 applications in metabolite synthesis and natural product biosynthesis.

Main Results:

  • Engineered P450s demonstrate valuable non-natural catalytic activities.
  • P450s readily accept new substrates and exhibit altered selectivities upon mutation.
  • Active site properties, including nonpolarity and conformational variability, contribute to P450 evolvability.

Conclusions:

  • Protein engineering has unlocked significant potential for P450 enzymes in biocatalysis.
  • The inherent evolvability of P450s makes them powerful tools for synthetic chemistry.
  • Understanding P450 structural dynamics is key to further optimizing their catalytic capabilities.