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Transglutaminase factor XIII uses proteinase‐like catalytic triad to crosslink macromolecules
Author(s) -
Pedersen Lars C.,
Yee Vivien C.,
Bishop Paul D.,
Trong Isolde Le,
Teller David C.,
Stenkamp Ronald E.
Publication year - 1994
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560030720
Subject(s) - tissue transglutaminase , cysteine , active site , proteolysis , catalytic triad , enzyme , chemistry , macromolecule , biochemistry , triad (sociology) , protein structure , stereochemistry , psychology , psychoanalysis
The X‐ray crystal structure of human transglutaminase factor XIII has revealed a cysteine proteinase‐like active site involved in a crosslinking reaction and not proteolysis. This is among the first observations of similar active sites in 2 different enzyme families catalyzing a similar reaction in opposite directions. Although the size and overall protein fold of factor XIII and the cysteine proteinases are quite different, the active site and the surrounding protein structure share structural features suggesting a common evolutionary lineage. Here we present a description of the residues in the active site and the structural evidence that the catalytic mechanism of the transglutaminases is similar to the reverse mechanism of the cysteine proteinases.