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Related Concept Videos

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...
Ribozymes02:47

Ribozymes

The term ribozyme is used for RNA that can act as an enzyme. Ribozymes are mainly found in selected viruses, bacteria, plant organelles, and lower eukaryotes. Ribozymes were first discovered in 1982 when Tom Cech’s laboratory observed Group I introns acting as enzymes. This was shortly followed by the discovery of another ribozyme, Ribonulcease P, by Sid Altman’s laboratory. Both Cech and Altman received the Nobel Prize in chemistry in 1989 for their work on ribozymes.
Ribozymes can be...
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.
Ribozymes02:47

Ribozymes

The term ribozyme is used for RNA that can act as an enzyme. Ribozymes are mainly found in selected viruses, bacteria, plant organelles, and lower eukaryotes. Ribozymes were first discovered in 1982 when Tom Cech’s laboratory observed Group I introns acting as enzymes. This was shortly followed by the discovery of another ribozyme, Ribonulcease P, by Sid Altman’s laboratory. Both Cech and Altman received the Nobel Prize in chemistry in 1989 for their work on ribozymes.
Ribozymes can be...
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...

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Multi-enzyme Screening Using a High-throughput Genetic Enzyme Screening System
08:10

Multi-enzyme Screening Using a High-throughput Genetic Enzyme Screening System

Published on: August 8, 2016

Metamorphic enzyme assembly in polyketide diversification.

Liangcai Gu1, Bo Wang, Amol Kulkarni

  • 1Life Sciences Institute, Department of Medicinal Chemistry, University of Michigan, Ann Arbor, Michigan 48109, USA.

Nature
|June 5, 2009
PubMed
Summary
This summary is machine-generated.

Enzymes in Lyngbya majuscula evolved parallel pathways to create unique chemical structures like cyclopropane and vinyl chloride. This study reveals how enzyme modifications drive natural product diversity.

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Area of Science:

  • Biochemistry
  • Natural Product Biosynthesis
  • Enzymology
  • Chemical Biology

Background:

  • Natural product diversity arises from evolving biosynthetic pathways in secondary metabolism.
  • The co-evolution of enzymes driving metabolic diversification remains poorly understood at the biochemical level.
  • Lyngbya majuscula produces complex secondary metabolites through intricate enzymatic processes.

Purpose of the Study:

  • To biochemically investigate the mechanisms of cyclopropane and vinyl chloride formation in Lyngbya majuscula.
  • To understand the co-evolution of enzymes involved in polyketide beta-branching and halogenation.
  • To elucidate the parallel evolutionary events leading to functional group diversity in secondary metabolites.

Main Methods:

  • Biochemical assessment of key enzymes including halogenase, dehydratases (ECH(1)s), decarboxylases (ECH(2)s), and enoyl reductase domains.
  • Analysis of parallel biosynthetic pathways (Curacin A and Jamaicamide pathways) from Lyngbya majuscula.
  • Characterization of enzyme activities in the formation of beta-branched cyclopropane and vinyl chloride moieties.

Main Results:

  • A halogenase introduced a gamma-chlorination step in the polyketide beta-branching pathway.
  • Divergent activities of ECH(2) enzymes led to either alpha,beta or beta,gamma enoyl thioester formation.
  • An enoyl reductase domain catalyzed an unprecedented cyclopropanation reaction, forming a cyclopropane ring.

Conclusions:

  • The combination of chlorination, polyketide beta-branching, and enzyme mechanistic diversification generates cyclopropane and vinyl chloride moieties.
  • Parallel evolution in multienzyme systems drives functional group diversity in natural products.
  • This study provides biochemical insights into the co-evolution of enzymes for metabolic diversification.