JBC Connect with Cosmo for Collagen Detection

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Sánchez, L. B.
Right arrow Articles by Müller, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Sánchez, L. B.
Right arrow Articles by Müller, M.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

J Biol Chem, Vol. 275, Issue 8, 5794-5803, February 25, 2000

Acetyl-CoA Synthetase from the Amitochondriate Eukaryote Giardia lamblia Belongs to the Newly Recognized Superfamily of Acyl-CoA Synthetases (Nucleoside Diphosphate-forming)*

Lidya B. SánchezDagger §, Michael Y. Galperin, and Miklós MüllerDagger

From Dagger  The Rockefeller University, New York, New York 10021 and  National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, Maryland 20894

The gene coding for the acetyl-CoA synthetase (ADP-forming) from the amitochondriate eukaryote Giardia lamblia has been expressed in Escherichia coli. The recombinant enzyme exhibited the same substrate specificity as the native enzyme, utilizing acetyl-CoA and adenine nucleotides as preferred substrates and less efficiently, propionyl- and succinyl-CoA. N- and C-terminal parts of the G. lamblia acetyl-CoA synthetase sequence were found to be homologous to the alpha - and beta -subunits, respectively, of succinyl-CoA synthetase. Sequence analysis of homologous enzymes from various bacteria, archaea, and the eukaryote, Plasmodium falciparum, identified conserved features in their organization, which allowed us to delineate a new superfamily of acyl-CoA synthetases (nucleoside diphosphate-forming) and its signature motifs. The representatives of this new superfamily of thiokinases vary in their domain arrangement, some consisting of separate alpha - and beta -subunits and others comprising fusion proteins in alpha -beta or beta -alpha orientation. The presence of homologs of acetyl-CoA synthetase (ADP-forming) in such human pathogens as G. lamblia, Yersinia pestis, Bordetella pertussis, Pseudomonas aeruginosa, Vibrio cholerae, Salmonella typhi, Porphyromonas gingivalis, and the malaria agent P. falciparum suggests that they might be used as potential drug targets.

* This research was supported in part by National Institutes of Health Grant AI11942 (to M. M.) and the NCBI, National Institutes of Health Visitors Program (to L. S.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ To whom correspondence should be addressed: The Rockefeller University, 1230 York Avenue, New York, NY 10021. Tel.: 212-327-8144; Fax: 212-327-7974; E-mail: sanchel@rockvax.rockefeller.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
C. Brasen, M. Schmidt, J. Grotzinger, and P. Schonheit
Reaction Mechanism and Structural Model of ADP-forming Acetyl-CoA Synthetase from the Hyperthermophilic Archaeon Pyrococcus furiosus: EVIDENCE FOR A SECOND ACTIVE SITE HISTIDINE RESIDUE
J. Biol. Chem., May 30, 2008; 283(22): 15409 - 15418.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
K. Shikata, T. Fukui, H. Atomi, and T. Imanaka
A Novel ADP-forming Succinyl-CoA Synthetase in Thermococcus kodakaraensis Structurally Related to the Archaeal Nucleoside Diphosphate-forming Acetyl-CoA Synthetases
J. Biol. Chem., September 14, 2007; 282(37): 26963 - 26970.
[Abstract] [Full Text] [PDF]

Home page
 Microbiol. Mol. Biol. Rev.Home page
A. J. Wolfe
The Acetate Switch
Microbiol. Mol. Biol. Rev., March 1, 2005; 69(1): 12 - 50.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
J. M. Shockey, M. S. Fulda, and J. Browse
Arabidopsis Contains a Large Superfamily of Acyl-Activating Enzymes. Phylogenetic and Biochemical Analysis Reveals a New Class of Acyl-Coenzyme A Synthetases
Plant Physiology, June 1, 2003; 132(2): 1065 - 1076.
[Abstract] [Full Text] [PDF]

Home page
 Genome ResHome page
D. A. Rodionov, A. A. Mironov, and M. S. Gelfand
Conservation of the Biotin Regulon and the BirA Regulatory Signal in Eubacteria and Archaea
Genome Res., October 1, 2002; 12(10): 1507 - 1516.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
B. L. Fatland, J. Ke, M. D. Anderson, W. I. Mentzen, L. W. Cui, C. C. Allred, J. L. Johnston, B. J. Nikolau, and E. S. Wurtele
Molecular Characterization of a Heteromeric ATP-Citrate Lyase That Generates Cytosolic Acetyl-Coenzyme A in Arabidopsis
Plant Physiology, October 1, 2002; 130(2): 740 - 756.
[Abstract] [Full Text] [PDF]

Home page
 Appl. Environ. Microbiol.Home page
E. Masai, K. Harada, X. Peng, H. Kitayama, Y. Katayama, and M. Fukuda
Cloning and Characterization of the Ferulic Acid Catabolic Genes of Sphingomonas paucimobilis SYK-6
Appl. Envir. Microbiol., September 1, 2002; 68(9): 4416 - 4424.
[Abstract] [Full Text] [PDF]

Home page
 Eukaryot CellHome page
J. E. J. Nixon, A. Wang, J. Field, H. G. Morrison, A. G. McArthur, M. L. Sogin, B. J. Loftus, and J. Samuelson
Evidence for Lateral Transfer of Genes Encoding Ferredoxins, Nitroreductases, NADH Oxidase, and Alcohol Dehydrogenase 3 from Anaerobic Prokaryotes to Giardialamblia and Entamoebahistolytica
Eukaryot. Cell, April 1, 2002; 1(2): 181 - 190.
[Abstract] [Full Text] [PDF]

Home page
 J. Bacteriol.Home page
M. Musfeldt and P. Schonheit
Novel Type of ADP-Forming Acetyl Coenzyme A Synthetase in Hyperthermophilic Archaea: Heterologous Expression and Characterization of Isoenzymes from the Sulfate Reducer Archaeoglobus fulgidus and the Methanogen Methanococcus jannaschii
J. Bacteriol., February 1, 2002; 184(3): 636 - 644.
[Abstract] [Full Text] [PDF]

Home page
 Microbiol. Mol. Biol. Rev.Home page
C. C. Hase, N. D. Fedorova, M. Y. Galperin, and P. A. Dibrov
Sodium Ion Cycle in Bacterial Pathogens: Evidence from Cross-Genome Comparisons
Microbiol. Mol. Biol. Rev., September 1, 2001; 65(3): 353 - 370.
[Abstract] [Full Text] [PDF]

Home page
 Clin. Microbiol. Rev.Home page
R. D. Adam
Biology of Giardia lamblia
Clin. Microbiol. Rev., July 1, 2001; 14(3): 447 - 475.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2000 by the American Society for Biochemistry and Molecular Biology.