The role of arginine residues at enzyme active sites. The interaction between guanidinium ions and p-nitro-phenyl phosphate and its effect on the rate of hydrolysis of the ester.
Biochim Biophys Acta
; 481(1): 1-5, 1977 Mar 15.
Article
de En
| MEDLINE
| ID: mdl-843535
ABSTRACT
In alcoholic solutions a relatively strong complex forms among two guanidinium ions and one p-nitrophenylphosphate dianion. The effect of this complex formation on the hydrolysis of the ester is to lower the rate by a factor of 4 in solutions containing 1 M guanidine hydrochloride when compared with solutions of the same total ionic strength containing no guanidinium ion. It is therefore suggested that, for the enzymatically catalyzed hydrolysis of phosphate compounds going via the formation of a metaphosphate intermediate, the role of any arginine residues at the active site is primarily one of binding and positioning the substrate.
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Collection:
01-internacional
Base de données:
MEDLINE
Sujet principal:
Phosphates
/
Arginine
/
Sites de fixation
/
Enzymes
/
Guanidines
Langue:
En
Journal:
Biochim Biophys Acta
Année:
1977
Type de document:
Article