On the similar spatial arrangement of active site residues in PAPS-dependent and phenolic sulfate-utilizing sulfotransferases.
FEBS Lett
; 583(18): 3091-4, 2009 Sep 17.
Article
em En
| MEDLINE
| ID: mdl-19695253
ABSTRACT
Mammalian sulfotransferases (STs) utilize exclusively the sulfuryl group donor 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to catalyze the sulfurylation reactions based on a sequential transfer mechanism. In contrast, the commensal intestinal bacterial arylsulfate sulfotransferases (ASSTs) do not use PAPS as the sulfuryl group donor, but instead catalyze sulfuryl transfer from phenolic sulfate to a phenol via a Ping-Pong mechanism. Interestingly, structural comparison revealed a similar spatial arrangement of the active site residues as well as the cognate substrates in mouse ST (mSULT1D1) and Escherichia coli CFT073 ASST, despite that their overall structures bear no discernible relationship. These observations suggest that the active sites of PAPS-dependent SULT1D1 and phenolic sulfate-utilizing ASST represent an example of convergent evolution.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Fosfoadenosina Fosfossulfato
/
Arilsulfotransferase
/
Domínio Catalítico
Limite:
Animals
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
2009
Tipo de documento:
Article