Papers

Peer-reviewed
Mar, 2006

On the interaction site of serine acetyltransferase in the cysteine synthase complex from Escherichia coli

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
  • CH Zhao
    • ,
  • Y Moriga
    • ,
  • B Feng
    • ,
  • Y Kumada
    • ,
  • H Imanaka
    • ,
  • K Imamura
    • ,
  • K Nakanishi
Volume
341
Number
4
First page
911
Last page
916
Language
English
Publishing type
Research paper (scientific journal)
DOI
10.1016/j.bbrc.2006.01.054
Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
Cysteine synthase from Escherichia coli is a bienzyme complex comprised of serine acetyltransferase (SAT) and O-acetylserine sulfhydrylase A. The site of interaction of a SAT molecule was investigated by gel chromatography and surface plasmon technique using various mutant-type SATs, to better understand the mechanism involved in complex formation. The C-terminus of SAT, Ile 273, along with Glu 268 and Asp 271, was found to be essential for complex formation. The effects of O-acetyl-L-serine and sulfide on the affinity for the complex formation were also studied using a surface plasmon technique. (c) 2006 Elsevier Inc. All rights reserved.
Link information
DOI
https://doi.org/10.1016/j.bbrc.2006.01.054
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000235699900003&DestApp=WOS_CPL
ID information
  • DOI : 10.1016/j.bbrc.2006.01.054
  • ISSN : 0006-291X
  • Web of Science ID : WOS:000235699900003
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