In:
FEBS Letters, Wiley, Vol. 457, No. 3 ( 1999-09-03), p. 323-326
Abstract:
The chemotaxis response regulator CheY can acquire phosphoryl groups either from its associated autophosphorylating protein kinase, CheA, or from small phosphodonor molecules such as acetyl phosphate. We report a stopped‐flow kinetic analysis of CheY phosphorylation by acetyl phosphate. The results show that CheY has a very low affinity for this phosphodonor ( K s ≫0.1 M), consistent with the conclusion that, whereas CheY provides catalytic functions for the phosphotransfer reaction, the CheA kinase may act simply to increase the effective phosphodonor concentration at the CheY active site.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1016/S0014-5793(99)01057-1
Language:
English
Publisher:
Wiley
Publication Date:
1999
detail.hit.zdb_id:
1460391-3
SSG:
12
