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:

gabD - succinate-semialdehyde dehydrogenase I

Escherichia coli O157:H7 str. Sakai

Skinner, M.A. et al., Cozzani, I. et al., Söhling, B. et al., Valentin, H.E. 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.

Disease relevance of ECs3522

The gene region (6,575 bp) contained several open reading frames which encoded the coenzyme A (CoA)- and NADP+-dependent succinate-semialdehyde dehydrogenase (sucD), the 4-hydroxybutyrate dehydrogenase (4hbD), and a succinyl-CoA;CoA transferase (cat1), as analyzed by heterologous expression in E. coli [1].

High impact information on ECs3522

Enzymic studies also provided evidence for the presence of an active succinate-semialdehyde dehydrogenase in 4-hydroxybutyrate-grown cells [2].
When the mutants are grown with 4-aminobutyrate as sole nitrogen source an NAD-dependent succinate semialdehyde dehydrogenase seen in the parental strain is absent but, as in the parental strain, an NADP-dependent enzyme is induced [3].
Escherichia coli mutants, unable to grow on 4-hydroxyphenylacetate, have been isolated and found to be defective in the NAD-dependent succinate semialdehyde dehydrogenase [3].
Separation and characterization of NAD- and NADP-specific succinate-semialdehyde dehydrogenase from Escherichia coli K-12 3300 [4].

Analytical, diagnostic and therapeutic context of ECs3522

Two distinct proteins endowed with succinate-semialdehyde dehydrogenase (succinate-semialdehyde:NAD(P)+oxidoreductase, EC 1.2.1.16) activity were separated and partially purified by ammonium sulphate fractionation or Sephadex G-200 gel-filtration or both [4].

References

Molecular analysis of the anaerobic succinate degradation pathway in Clostridium kluyveri. Söhling, B., Gottschalk, G. J. Bacteriol. (1996) [Pubmed]
Metabolic pathway for biosynthesis of poly(3-hydroxybutyrate-co-4-hydroxybutyrate) from 4-hydroxybutyrate by Alcaligenes eutrophus. Valentin, H.E., Zwingmann, G., Schönebaum, A., Steinbüchel, A. Eur. J. Biochem. (1995) [Pubmed]
An Escherichia coli mutant defective in the NAD-dependent succinate semialdehyde dehydrogenase. Skinner, M.A., Cooper, R.A. Arch. Microbiol. (1982) [Pubmed]
Separation and characterization of NAD- and NADP-specific succinate-semialdehyde dehydrogenase from Escherichia coli K-12 3300. Cozzani, I., Fazio, A.M., Felici, E., Barletta, G. Biochim. Biophys. Acta (1980) [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