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Inter‐ and intramolecular domain interactions of the catalase‐peroxidase KatG from M. tuberculosis
Author(s) -
Wilming Martin,
Johnsson Kai
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)03179-9
Subject(s) - intramolecular force , catalase , peroxidase , chemistry , mycobacterium tuberculosis , enzyme , domain (mathematical analysis) , stereochemistry , amino acid , biochemistry , tuberculosis , medicine , mathematical analysis , mathematics , pathology
The inter‐ and intramolecular 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 addition, an intramolecular interaction between the N‐ and C‐terminal domains was detected which might play a functional role in the mechanism of the enzyme.