Alteration of the quaternary structure of human UDP-glucose dehydrogenase by a double mutation.
J Biochem Mol Biol
; 40(5): 690-6, 2007 Sep 30.
Article
em En
| MEDLINE
| ID: mdl-17927902
ABSTRACT
There are conflicting views for the polymerization process of human UDP-glucose dehydrogenase (UGDH) and no clear evidence has been reported yet. Based on crystal coordinates for Streptococcus pyogenes UGDH, we made double mutant A222Q/S233G. The double mutagenesis had no effects on expression, stability, and secondary structure. Interestingly, A222Q/S233G was a dimeric form and showed an UGDH activity, although it showed increased Km values for substrates. These results suggest that Ala222 and Ser233 play an important role in maintaining the hexameric structure and the reduced binding affinities for substrates are attributable to its altered subunit communication although quaternary structure may not be critical for catalysis.
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Bases de dados:
MEDLINE
Assunto principal:
Uridina Difosfato Glucose Desidrogenase
/
Mutação
Limite:
Humans
Idioma:
En
Revista:
J Biochem Mol Biol
Assunto da revista:
BIOLOGIA MOLECULAR
/
BIOQUIMICA
Ano de publicação:
2007
Tipo de documento:
Article