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Catalytically Perfect Enzymes01:07

Catalytically Perfect Enzymes

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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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Introduction to Enzymes01:22

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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.’
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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.
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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.
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Introduction to Enzyme Kinetics01:19

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Enzyme kinetics studies the rates of biochemical reactions. Scientists monitor the reaction rates for a particular enzymatic reaction at various substrate concentrations. Additional trials with inhibitors or other molecules that affect the reaction rate may also be performed.
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Biosynthesis of a Flavonol from a Flavanone by Establishing a One-pot Bienzymatic Cascade
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Flavoenzymes for biocatalysis.

Mélanie Hall1

  • 1Department of Chemistry, University of Graz, Graz, Austria.

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Summary
This summary is machine-generated.

Flavoenzymes, crucial biocatalysts, utilize reduced flavin cofactors and nicotinamide reductants for diverse reactions like oxidation and hydrogenation. These enzymes offer superior regio-, chemo-, and stereo-selectivity for synthesizing chiral molecules.

Keywords:
BiocatalysisCarboxylationEpoxidationMonooxygenationOrganic synthesisReductionStereoselectivity

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Area of Science:

  • Biocatalysis
  • Enzymology
  • Organic Chemistry

Background:

  • Flavoenzymes are versatile biocatalysts due to their flavin cofactor.
  • Many flavoenzymes require nicotinamide adenine dinucleotide (phosphate) (NAD(P)H) as an electron source for catalysis.
  • Reduced flavins are reactive with oxygen for monooxygenation and can perform hydrogenation reactions.

Purpose of the Study:

  • To provide an overview of biocatalytic processes using flavoenzymes.
  • To focus on nicotinamide-dependent flavoenzymes.
  • To highlight the diversity of products and stereochemical control strategies.

Main Methods:

  • Review of literature on flavoenzyme biocatalysis.
  • Analysis of reactions including monooxygenation and hydrogenation.
  • Examination of stereochemical control in flavoenzyme-catalyzed reactions.

Main Results:

  • Flavoenzymes catalyze a wide array of reactions with high selectivity.
  • Nicotinamide-dependent flavoenzymes are key biocatalysts for various transformations.
  • Strategies for controlling stereochemical outcomes in biocatalytic synthesis are effective.

Conclusions:

  • Flavoenzymes offer environmentally friendly and selective alternatives to chemical catalysts.
  • The application of flavoenzymes, particularly nicotinamide-dependent ones, is expanding in biocatalysis.
  • Precise stereochemical control is achievable using flavoenzyme-mediated synthesis.