Different Enzymatic Processing of γ-Phosphoramidate and γ-Phosphoester-Modified ATP Analogues.
Chembiochem
; 18(4): 378-381, 2017 02 16.
Article
em En
| MEDLINE
| ID: mdl-27935244
ABSTRACT
Monitoring the activity of ATP-consuming enzymes provides the basis for elucidating their modes of action and regulation. Although a number of ATP analogues have been developed for this, their scope is restricted because of the limited acceptance by respective enzymes. In order to clarify which kind of phosphate-modified ATP analogues are accepted by the α-ß-phosphoanhydride-cleaving ubiquitin-activating enzymeâ
1 (UBA1) and the ß-γ-phosphoanhydride-cleaving focal adhesion kinase (FAK), we tested phosphoramidate- and phosphoester-modified ATP analogues. UBA1 and FAK were able to convert phosphoramidate-modified ATP analogues, even with a bulky modification like biotin. In contrast, a phosphoester-modified analogue was poorly accepted. These results demonstrate that minor variations in the design of ATP analogues for monitoring ATP utilization have a significant impact on enzymatic acceptance.
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Ácidos Fosfóricos
/
Trifosfato de Adenosina
/
Enzimas
/
Ésteres
/
Amidas
Idioma:
En
Ano de publicação:
2017
Tipo de documento:
Article