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Related Concept Videos

Sulfur Assimilation01:20

Sulfur Assimilation

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Sulfur is an essential element in biological systems, contributing to synthesizing key biomolecules, including amino acids such as cysteine and methionine, and cofactors such as coenzyme A and biotin. Microorganisms primarily assimilate sulfur as sulfate (SO₄²⁻) from the environment, which must undergo a series of biochemical transformations before it can be incorporated into cellular components. As sulfate is highly oxidized, it must undergo assimilatory sulfate reduction to...
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Salt stress—which can be triggered by high salt concentrations in a plant’s environment—can significantly affect plant growth and crop production by influencing photosynthesis and the absorption of water and nutrients.
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Most plants use the C3 pathway for carbon fixation. However, some plants, such as sugar cane, corn, and cacti that grow in hot conditions, use alternative pathways to fix carbon and conserve energy loss due to photorespiration. Photorespiration is the process that occurs when the oxygen concentration is high. Under such conditions, the rubisco enzyme in the Calvin cycle binds O2 instead of CO2, which halts photosynthesis and consumes energy.
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Phase II Reactions: Sulfation and Conjugation with α-Amino Acids01:19

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Sulfation and α-amino acid conjugation are two critical biotransformation reactions in drug metabolism. Sulfation, a phase II biotransformation reaction, involves adding a polar sulfate group to a drug, enhancing its water solubility and promoting excretion. This process can either co-occur with or occur independently of glucuronidation. Nonmicrosomal sulfotransferase enzymes catalyze the process. The reaction involves 3'-phosphoadenosine-5'-phosphosulfate or PAPS coenzyme...
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Phase II reactions are essential for the detoxification and elimination of drugs from the body. These reactions involve the conjugation of parent drugs or their phase I metabolites with endogenous molecules, resulting in more hydrophilic drug conjugates. The primary conjugation reactions in this phase are sulfation and glucuronidation. Both sulfation and glucuronidation typically produce biologically inactive metabolites. However, in some cases involving prodrugs, active metabolites may be...
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Ribulose 1,5- bisphosphate carboxylase/oxygenase (RuBisCo) is a critical enzyme that catalyzes carbon dioxide assimilation during photosynthesis. However, it is an inefficient enzyme, having an extremely slow catalytic rate. A typical enzyme can process about a thousand molecules per second; however, RuBisCo fixes only around three-carbon dioxides per second. Photosynthetic cells compensate for this slow rate by synthesizing very high amounts of RuBisCo, making it the most abundant single...
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Related Experiment Video

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Detection of Histone Modifications in Plant Leaves
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Sulphate activation in higher plants.

R J Ellis1

  • 1Department of Botany, University of Aberdeen, Aberdeen, Scotland.

Planta
|February 8, 2014
PubMed
Summary
This summary is machine-generated.

ATP-sulphurylase, crucial for sulfate reduction in plants, functions optimally at pH 8.0 with Mg2+ ions. Unlike microorganisms, its synthesis is not regulated by sulfate or cystine levels, suggesting a unique plant pathway.

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Area of Science:

  • Plant Biochemistry
  • Enzymology
  • Sulfate Metabolism

Background:

  • Sulfate assimilation is a vital process in plants, providing sulfur for amino acids and other essential molecules.
  • The initial steps of sulfate reduction involve enzymatic activation and subsequent reduction.
  • Understanding these pathways is key to improving plant nutrition and stress tolerance.

Purpose of the Study:

  • To characterize the enzyme ATP-sulphurylase in higher plants.
  • To investigate the regulatory mechanisms of sulfate assimilation in plants.
  • To elucidate the pathway of sulfate reduction in plant tissues.

Main Methods:

  • Enzyme assays on plant extracts (roots and leaves).
  • Determination of optimal pH and cofactor requirements (Mg2+).
  • Testing inhibitors (selenate, molybdate, amino acids, thiol reagents).
  • Aseptic cultivation of plants to study enzyme synthesis regulation.

Main Results:

  • ATP-sulphurylase was identified in plant supernatants, with a pH optimum of 8.0 and requiring Mg2+.
  • Enzyme activity was inhibited by selenate and molybdate but not by sulfur-containing amino acids or thiol reagents.
  • Plant ATP-sulphurylase synthesis was not induced by sulfate or repressed by cystine.
  • APS-kinase was undetectable, and its product was stable, suggesting it's not involved in the primary pathway.

Conclusions:

  • Higher plants likely reduce sulfate via adenylylsulfate (APS), not phosphoadenylylsulfate (PAPS) as seen in many microbes.
  • Plant sulfate assimilation regulation differs significantly from microbial systems.
  • The findings provide insights into the unique biochemical pathways of sulfur metabolism in plants.