Transglutaminase factor XIII uses proteinase-like catalytic triad to crosslink macromolecules.
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.
Pedersen
L C
LC
Department of Biochemistry, University of Washington, Seattle 98195.
Yee
V C
VC
Bishop
P D
PD
Le Trong
I
I
Teller
D C
DC
Stenkamp
R E
RE
D001665:Binding Sites; D003432:Cross-Linking Reagents; D003460:Crystallization; D018360:Crystallography, X-Ray; D003546:Cysteine Endopeptidases / Q000737:chemistry* / Q000378:metabolism; D005176:Factor XIII / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D015394:Molecular Structure; D011503:Transglutaminases / Q000737:chemistry* / Q000378:metabolism
D003432:Cross-Linking Reagents; D005176:Factor XIII; D011503:Transglutaminases; D003546:Cysteine Endopeptidases