NISCAIR Online Periodicals Repository

Research Journals >
Indian Journal of Experimental Biology (IJEB) >
IJEB Vol.44 [2006] >
IJEB Vol.44(09) [September 2006] >

Title: Catalytic and regulatory properties of sulphur metabolizing enzymes in cyanobacterium Synechococcus elongatus PCC 7942
Authors: Jain, Anuradha
Verma, Deepti
Bagchi, Divya
Keywords: Catalytic property
Regulatory property
Sulphur metabolizing enzyme
Synechococcus elongatus
Issue Date: Sep-2006
Publisher: CSIR
Abstract: Synechococcus elongatus PCC 7942 was able to grow with several S sources. The sulphur metabolizing enzymes viz. ATP sulphurylase, cysteine synthase, thiosulphate reductase and L- and D-cysteine desulphydrases were regulated by sulphur sources, particularly by sulphur amino acids and organic sulphate esters. Sulphur starvation reduced ATP sulphurylase and cysteine synthase whereas reduced glutathione appreciated Cys degradation activity. With partially purified enzymes apparent Km values for sulphate, ATP, D- and L-Cys, thiosulphate, sulphide and O-acetyl serine were in a range of 12-50 ยตM. p-Nitrophenyl sulphate inhibited ATP sulphurylase competitively. Met was a feedback inhibitor of several key enzymes.
Page(s): 767-772
ISSN: 0975-1009 (Online); 0019-5189 (Print)
Source:IJEB Vol.44(09) [September 2006]

Files in This Item:

File Description SizeFormat
IJEB 44(9) 767-772.pdf232.84 kBAdobe PDFView/Open
 Current Page Visits: 70 
Recommend this item


Online Submission of Articles |  NISCAIR Website |  National Knowledge Resources Consortium |  Contact us |  Feedback

Disclaimer: NISCAIR assumes no responsibility for the statements and opinions advanced by contributors. The editorial staff in its work of examining papers received for publication is helped, in an honorary capacity, by many distinguished engineers and scientists.

CC License Except where otherwise noted, the Articles on this site are licensed under Creative Commons License: CC Attribution-Noncommercial-No Derivative Works 2.5 India

Copyright © 2015 The Council of Scientific and Industrial Research, New Delhi. All rights reserved.

Powered by DSpace Copyright © 2002-2007 MIT and Hewlett-Packard | Compliant to OAI-PMH V 2.0

Home Page Total Visits: 161957 since 01-Sep-2015  Last updated on 21-Jun-2016Webmaster: