Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Editor

Personal info

View

About

Terms

Javascript disabled

Please enable Javascript support in your browser to use this application.

Instructions on how to enable JavaScript on different browsers can be found here: http://www.google.com/support/bin/answer.py?answer=23852.

[edit this page]

Gene Review:

ECs1473 - 3-oxoacyl-ACP synthase

Escherichia coli O157:H7 str. Sakai

Olsen, J.G. et al., Arnvig Mcguire, K. et al., Schütt, B.S. et al., Jones, A.L. et al., Subrahmanyam, S. et al.

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

High impact information on ECs1473

Incubations with chloroplasts and direct assay of the individual condensing enzymes showed that all three compounds inhibited the pea FAS condensing enzymes in the order KAS II > KAS I > KAS III [1].
The amino acid sequence deduced from clKAS IV cDNA showed 80% identity to other plant KAS II-type enzymes, 55% identity towards plant KAS I and over 90% towards other Cuphea KAS IV-type sequences [2].
Malonyl-CoA increased to about 40% of the total cellular CoA pool upon KAS II overproduction from a steady-state level of around 0.5% in the absence of KAS II overproduction [3].
CONCLUSIONS: The same mechanism is proposed for KAS II, which also has a Cys-His-His active site triad [4].
The acyl binding pockets of KAS I and KAS II are so similar that they alone cannot provide the basis for their differences in substrate specificity [4].

Associations of ECs1473 with chemical compounds

Analyses using the cross-linker BS(3) [bis(sulphosuccinimidyl) suberate] and surface-enhanced laser desorption/ionization-time-of-flight MS disclosed only monomeric and dimeric forms of KAS II, whereas KAS I also forms higher multimers [5].

References

Novel inhibitors of the condensing enzymes of the type II fatty acid synthase of pea (Pisum sativum). Jones, A.L., Herbert, D., Rutter, A.J., Dancer, J.E., Harwood, J.L. Biochem. J. (2000) [Pubmed]
Beta-ketoacyl-acyl carrier protein synthase IV: a key enzyme for regulation of medium-chain fatty acid synthesis in Cuphea lanceolata seeds. Schütt, B.S., Abbadi, A., Loddenkötter, B., Brummel, M., Spener, F. Planta (2002) [Pubmed]
Overproduction of a functional fatty acid biosynthetic enzyme blocks fatty acid synthesis in Escherichia coli. Subrahmanyam, S., Cronan, J.E. J. Bacteriol. (1998) [Pubmed]
Structures of beta-ketoacyl-acyl carrier protein synthase I complexed with fatty acids elucidate its catalytic machinery. Olsen, J.G., Kadziola, A., von Wettstein-Knowles, P., Siggaard-Andersen, M., Larsen, S. Structure (Camb.) (2001) [Pubmed]
Acyl carrier protein (ACP) inhibition and other differences between beta-ketoacyl synthase (KAS) I and II. Arnvig Mcguire, K., McGuire, J.N., von Wettstein-Knowles, P. Biochem. Soc. Trans. (2000) [Pubmed]

Contributions to this collaborative article are from individual authors of WikiGenes or mined by the WikiGenes Data Mining Engine from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenes Open Access Licence Privacy Policy Terms of Use apsburg

The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.