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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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Biosynthesis of Polysaccharides01:26

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Polysaccharides such as glycogen and starch are synthesized from nucleoside diphosphate sugars, primarily uridine diphosphate glucose (UDPG) and adenosine diphosphate glucose (ADPG). These activated glucose donors act as key intermediates in carbohydrate metabolism and biosynthesis. UDPG primarily involves glycogen synthesis in animals and many bacteria, while ADPG plays a fundamental role in starch synthesis in plants and certain bacteria.UDPG is formed when glucose-1-phosphate reacts with...
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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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Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
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Red algae, also known as rhodophytes, are primarily found in marine environments, though some species inhabit freshwater and terrestrial ecosystems. These organisms exist in both unicellular and multicellular forms, with some multicellular varieties reaching macroscopic sizes.As phototrophic organisms, red algae contain chlorophyll a; however, their chloroplasts lack chlorophyll b. Instead, they possess phycobiliproteins, which serve as major light-harvesting pigments, similar to those found in...
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Green Algae01:21

Green Algae

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Green algae, also referred to as chlorophytes, are different from red algae in having the chloroplasts containing chlorophylls a and b, which give them their distinct green hue. However, they lack phycobiliproteins, preventing them from developing the red or blue-green pigmentation seen in red algae. In terms of photosynthetic pigment composition, green algae closely resemble plants and share a close evolutionary relationship with them. Taxonomically Green algae belong to Phylum Chlorophyta in...
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Sulfatases: Critical Enzymes for Algal Polysaccharide Processing.

Andrew G Hettle1, Chelsea J Vickers2, Alisdair B Boraston1

  • 1Department of Biochemistry and Microbiology, University of Victoria, Victoria, BC, Canada.

Frontiers in Plant Science
|May 16, 2022
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Marine microbial sulfatases are key enzymes for breaking down algal polysaccharides. Understanding their structure and function is vital for marine carbon cycling and developing new biocatalysts.

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Area of Science:

  • Marine microbiology
  • Biocatalysis
  • Enzymology

Background:

  • Microbial sulfatases are crucial for marine carbon cycling.
  • They break down abundant sulphated algal polysaccharides like carrageenan, fucoidan, and ulvan.
  • These polysaccharides can represent up to 40% of marine biopolymer dry weight.

Purpose of the Study:

  • To review the S1 family of formylglycine-dependent sulfatases.
  • To emphasize recent developments in the structural and functional analysis of sulfatases acting on sulphated algal polysaccharides.
  • To highlight the role of sulfatases in marine carbon cycling and as biocatalysts.

Main Methods:

  • Review of recent literature on microbial sulfatases.
  • Analysis of structural and functional relationships between sulfatases and their polysaccharide substrates.
  • Utilisation of a recently proposed active site nomenclature for sulfatases.

Main Results:

  • The S1 family is the largest and most functionally diverse sulfatase family, often acting on polysaccharides.
  • Sulfatase-catalyzed hydrolysis is a key step in depolymerizing sulphated polysaccharides into metabolizable monosaccharides.
  • Recent studies provide insights into the structure-function relationships of these enzymes.

Conclusions:

  • Sulfatases play a critical role in marine ecosystems and carbon cycling.
  • Understanding sulfatase structure-function is essential for comprehending polysaccharide metabolism.
  • These enzymes are promising biocatalysts for producing valuable sulphated oligomers for pharmaceutical and cosmetic industries.