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Overview of Metabolism01:40

Overview of Metabolism

Living cells constantly carry out various chemical reactions which are necessary for their proper functioning. These reactions are interlinked to one another via multiple pathways. The collection of these chemical reactions is known as metabolism.
Plant Metabolism
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Overview of Nitrogen Metabolism

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Lifecycle of Erythrocytes

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Amino Acid Catabolism01:18

Amino Acid Catabolism

Microorganisms rely on proteins as an essential carbon and energy source, particularly in environments with limited polysaccharides or lipids. However, proteins are too large to cross the plasma membrane unaided, necessitating enzymatic degradation. Microbes secrete extracellular proteases and peptidases that hydrolyze proteins into peptides, which can then be transported across the membrane. Once inside the cell, intracellular proteases degrade these peptides into free amino acids, which...
Microbial Bioremediation of Pesticides01:28

Microbial Bioremediation of Pesticides

Pesticides often feature structurally complex chemical architectures, incorporating halogen groups and multiple aromatic rings. These characteristics confer high chemical stability, rendering many pesticides resistant to natural degradation processes. This resistance poses significant environmental concerns, as persistent pesticide residues can accumulate in ecosystems and affect non-target organisms.Despite the inherent stability of many pesticides, certain microorganisms possess the metabolic...
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Articles linked to this work by shared authors, journal, and citation graph.

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Same author

Enzymes: nature's nanomachines. Royal Irish Academy Medal Lecture.

Biochemical Society transactions·2001
Same author

Structure of human biliverdin IXbeta reductase, an early fetal bilirubin IXbeta producing enzyme.

Nature structural biology·2001
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Studies on the specificity of the tetrapyrrole substrate for human biliverdin-IXalpha reductase and biliverdin-IXbeta reductase. Structure-activity relationships define models for both active sites.

The Journal of biological chemistry·2000
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Initial-rate kinetics of the flavin reductase reaction catalysed by human biliverdin-IXbeta reductase (BVR-B).

The Biochemical journal·2000
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The three-dimensional structure of a class-Pi glutathione S-transferase complexed with glutathione: the active-site hydration provides insights into the reaction mechanism.

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The three-dimensional structure of Cys-47-modified mouse liver glutathione S-transferase P1-1. Carboxymethylation dramatically decreases the affinity for glutathione and is associated with a loss of electron density in the alphaB-310B region.

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Related Experiment Video

Updated: Jul 24, 2026

Assaying Proteasomal Degradation in a Cell-free System in Plants
07:43

Assaying Proteasomal Degradation in a Cell-free System in Plants

Published on: March 26, 2014

Haem degradation in animals and plants.

T J Mantle1

  • 1Department of Biochemistry, Trinity College, Dublin 2, Ireland. tmantle@mail.tcd.ie

Biochemical Society Transactions
|August 28, 2002
PubMed
Summary

Two enzyme systems reduce linear tetrapyrroles. One system in plants and algae uses ferredoxin for chromophore synthesis, while another, biliverdin reductases, uses NAD(P)H to form bile pigments.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Linear tetrapyrroles are crucial biological molecules.
  • Enzymatic reduction pathways are essential for tetrapyrrole metabolism.
  • Diverse organisms possess distinct enzymatic systems for tetrapyrrole processing.

Purpose of the Study:

  • To delineate the two primary enzyme systems involved in linear tetrapyrrole reduction.
  • To differentiate the catalytic mechanisms and products of these two systems.
  • To understand the evolutionary divergence of tetrapyrrole reduction pathways.

Main Methods:

  • Comparative analysis of enzyme families.
  • Biochemical assays to determine substrate specificity and reaction products.
  • Spectroscopic methods to characterize chromophore formation.

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Measurement of Heme Synthesis Levels in Mammalian Cells
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Measurement of Heme Synthesis Levels in Mammalian Cells

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Identification of Pharmaceuticals in The Aquatic Environment Using HPLC-ESI-Q-TOF-MS and Elimination of Erythromycin Through Photo-Induced Degradation
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Identification of Pharmaceuticals in The Aquatic Environment Using HPLC-ESI-Q-TOF-MS and Elimination of Erythromycin Through Photo-Induced Degradation

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Last Updated: Jul 24, 2026

Assaying Proteasomal Degradation in a Cell-free System in Plants
07:43

Assaying Proteasomal Degradation in a Cell-free System in Plants

Published on: March 26, 2014

Measurement of Heme Synthesis Levels in Mammalian Cells
09:43

Measurement of Heme Synthesis Levels in Mammalian Cells

Published on: July 9, 2015

Identification of Pharmaceuticals in The Aquatic Environment Using HPLC-ESI-Q-TOF-MS and Elimination of Erythromycin Through Photo-Induced Degradation
05:46

Identification of Pharmaceuticals in The Aquatic Environment Using HPLC-ESI-Q-TOF-MS and Elimination of Erythromycin Through Photo-Induced Degradation

Published on: August 1, 2018

Main Results:

  • One enzyme family, utilizing ferredoxin, reduces terminal pyrrole rings (A and D) and vinyl side chains, producing light-harvesting and light-sensing chromophores in plants, algae, and cyanobacteria.
  • A second enzyme group, biliverdin reductases (A and B), employs NAD(P)H to catalyze reduction at C10 via hydride addition, yielding bile pigments like bilirubin-IX alpha and bilirubin-IX.

Conclusions:

  • Distinct evolutionary pathways have led to specialized enzyme systems for linear tetrapyrrole reduction.
  • These systems produce functionally diverse tetrapyrrole derivatives, essential for various biological processes.
  • Understanding these enzymatic mechanisms provides insight into pigment biosynthesis and metabolic diversity.