The structural basis for the remarkable catalytic proficiency of orotidine 5'-monophosphate decarboxylase.
Curr Opin Struct Biol
; 10(6): 711-8, 2000 Dec.
Article
em En
| MEDLINE
| ID: mdl-11114509
ABSTRACT
The three-dimensional structures of orotidine 5'-monophosphate decarboxylases from four different organisms have been determined by X-ray crystallography. The structures reveal an active site in which the pyrimidine base and phosphate groups are rigidly held in place. Surprisingly, both pyrimidine carbonyl groups are hydrogen bonded to amide groups, rather than to strong active site acids, as was previously predicted. The positioning of a conserved aspartate sidechain close to the substrate carboxylate and a conserved lysine ammonium group close to the C6 of the pyrimidine suggests a novel mechanism to explain the extreme catalytic proficiency of this enzyme.
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Base de dados:
MEDLINE
Assunto principal:
Orotidina-5'-Fosfato Descarboxilase
Idioma:
En
Ano de publicação:
2000
Tipo de documento:
Article