Transglutaminase factor XIII uses proteinase-like catalytic triad to crosslink macromolecules.
Protein Sci
; 3(7): 1131-5, 1994 Jul.
Article
em En
| MEDLINE
| ID: mdl-7920263
ABSTRACT
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.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Fator XIII
/
Cisteína Endopeptidases
/
Transglutaminases
Tipo de estudo:
Prognostic_studies
Idioma:
En
Revista:
Protein Sci
Assunto da revista:
BIOQUIMICA
Ano de publicação:
1994
Tipo de documento:
Article