Publication

Inter- and intramolecular domain interactions of the catalase-peroxidase KatG from M. tuberculosis

Kai Johnsson
2001
Journal Articles

Abstract

The inter- and intramol. interactions between the different domains of the catalase-peroxidase KatG from Mycobacterium tuberculosis were analyzed using the two-hybrid assay. It was shown that the dimerization of the enzyme is due to a strong interaction of the first 99 amino acids of the N-terminal domain whereas the C-terminal domain does not play a role in the dimerization. In addn., an intramol. interaction between the N- and C-terminal domains was detected which might play a functional role in the mechanism of the enzyme. [on SciFinder (R)]

Official source

https://infoscience.epfl.ch/entities/publication/8ff41790-efb7-4acc-9076-5dfe6de65856

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Kai Johnsson
2001
Journal Articles

Abstract

Official source

https://infoscience.epfl.ch/entities/publication/8ff41790-efb7-4acc-9076-5dfe6de65856

About this result

Related concepts (32)

Mycobacterium tuberculosis

Mycobacterium tuberculosis (M. tb), also known as Koch's bacillus, is a species of pathogenic bacteria in the family Mycobacteriaceae and the causative agent of tuberculosis. First discovered in 1882 by Robert Koch, M. tuberculosis has an unusual, waxy coating on its cell surface primarily due to the presence of mycolic acid. This coating makes the cells impervious to Gram staining, and as a result, M. tuberculosis can appear weakly Gram-positive. Acid-fast stains such as Ziehl–Neelsen, or fluorescent stains such as auramine are used instead to identify M.

Enzyme

Enzymes (ˈɛnzaɪmz) are proteins that act as biological catalysts by accelerating chemical reactions. The molecules upon which enzymes may act are called substrates, and the enzyme converts the substrates into different molecules known as products. Almost all metabolic processes in the cell need enzyme catalysis in order to occur at rates fast enough to sustain life. Metabolic pathways depend upon enzymes to catalyze individual steps.

Protein–protein interaction

Protein–protein interactions (PPIs) are physical contacts of high specificity established between two or more protein molecules as a result of biochemical events steered by interactions that include electrostatic forces, hydrogen bonding and the hydrophobic effect. Many are physical contacts with molecular associations between chains that occur in a cell or in a living organism in a specific biomolecular context. Proteins rarely act alone as their functions tend to be regulated.

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Inter- and intramolecular domain interactions of the catalase-peroxidase KatG from M. tuberculosis

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