Kinetics of CheY phosphorylation by small molecule phosphodonors

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...

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Veröffentlicht in:FEBS letters 1999-09, Vol.457 (3), p.323-326
Hauptverfasser: Da Re, Sandra S., Deville-Bonne, Dominique, Tolstykh, Tatiana, Véron, Michel, Stock, Jeffry B.
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container_issue 3
container_start_page 323
container_title FEBS letters
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creator Da Re, Sandra S.
Deville-Bonne, Dominique
Tolstykh, Tatiana
Véron, Michel
Stock, Jeffry B.
description 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.
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subjects AcP, acetyl phosphate
Amides - chemistry
Amides - metabolism
Bacterial Proteins
Biochemistry - instrumentation
Biochemistry - methods
Chemotaxis
Fluorescence
Histidine - analogs & derivatives
Histidine - metabolism
HPK, histidine protein kinase
Kinetics
Membrane Proteins - chemistry
Membrane Proteins - metabolism
Methyl-Accepting Chemotaxis Proteins
Organophosphates - chemistry
Organophosphates - metabolism
Pam, Phosphoramidate
Phosphoric Acids - chemistry
Phosphoric Acids - metabolism
Phosphorylation
Phosphotransfer
Two-component system
title Kinetics of CheY phosphorylation by small molecule phosphodonors
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