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Biotin ligase enzyme, molecular model

Biotin ligase enzyme, molecular model


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Biotin ligase enzyme, molecular model

Biotin ligase enzyme, molecular model. This enzyme is a protein formed from 268 amino acids and two chains (green and pink). This example is from the Mycobacterium tuberculosis bacterium that causes tuberculosis (TB). A ligase is an enzyme that catalyses a reaction joining two larger molecules together, such as proteins and DNA. In this case, the enzyme joins biotin to other chemicals, a process called biotinylation. Biotin is vitamin B7

Science Photo Library features Science and Medical images including photos and illustrations

Media ID 9220251

© LAGUNA DESIGN/SCIENCE PHOTO LIBRARY

Bacteria Bacteriology Biomolecule Biotin Enzyme Graphic Ligase Macromolecule Molecular Biology Molecules Mycobacterium Tuberculosis Proteins Proteomics Structural Tuberculosis Vitamin B7 Biochemical Biochemistry Cutouts Molecular Model Molecular Structure Protein


EDITORS COMMENTS
This print showcases the intricate molecular model of the Biotin ligase enzyme, derived from the Mycobacterium tuberculosis bacterium responsible for causing tuberculosis (TB). The enzyme itself is composed of two chains, depicted in vibrant green and pink hues, formed by a sequence of 268 amino acids. Against a striking black background, this illustration highlights the structural complexity and beauty found within biology. Ligases are essential enzymes that facilitate reactions between larger molecules, such as proteins and DNA. In this particular case, the Biotin ligase enzyme plays a crucial role in biotinylation - a process where it joins biotin to other chemicals. Biotin, also known as vitamin B7, holds significant importance in various biological processes. Through this visually stunning artwork created by Science Photo Library's talented team of experts in biochemistry and bacteriology, we gain an insight into the macromolecular world that underlies life itself. This image serves as a reminder of both the elegance and intricacy present within our natural world.

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