PMID:334767: Difference between revisions
Jump to navigation
Jump to search
New PMID: Page! |
Edited by wikibot |
||
| Line 1: | Line 1: | ||
{{RightTOC}} | {{RightTOC}} | ||
| Line 11: | Line 11: | ||
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=334767 PubMed] | |{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=334767 PubMed] | ||
|} | |} | ||
==Significance {{HelpIcon|Help:Literature}} == | ==Significance {{HelpIcon|Help:Literature}} == | ||
{{LitSignificance}} | {{LitSignificance}} | ||
| Line 19: | Line 19: | ||
==Annotations {{HelpIcon|Help:Literature}}== | ==Annotations {{HelpIcon|Help:Literature}}== | ||
<!--box uid=63ce1649aab8b3180235b0af7618f667.0.U47ab59b752f4e--> | |||
<!-- | <!-- | ||
****************************************************************************************** | ****************************************************************************************** | ||
| Line 32: | Line 32: | ||
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.U47ab59b752f4e&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || || | |[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.U47ab59b752f4e&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || || | ||
|} | |} | ||
<!--box uid=63ce1649aab8b3180235b0af7618f667.0.U47ab59b752f4e-- | <!--box uid=63ce1649aab8b3180235b0af7618f667.0.U47ab59b752f4e--> | ||
==EcoliWiki Links {{HelpIcon|Help:Literature}} == | ==EcoliWiki Links {{HelpIcon|Help:Literature}} == | ||
Revision as of 22:44, 25 April 2008
Dautry-Varsat, A and Cohen, GN (1977) Proteolysis of the bifunctional methionine-repressible aspartokinase II-homoserine dehydrogenase II of Escherichia coli K12. Production of an active homoserine dehydrogenase fragment.J. Biol. Chem. 252:7685-9
| Abstract | The dimeric bifunctional enzyme aspartokinase II-homoserine dehydrogenase II (Mr = 2 X 88,000) of Escherichia coli K12 can be cleaved into two nonoverlapping fragments by limited proteolysis with subtilisin. These two fragments can be separated under nondenaturing conditions as dimeric species, which indicates that each fragment has retained some of the association areas involved in the conformation of the native protein. The smaller fragment (Mr = 2 X 24,000) is devoid of aspartokinase and homoserine dehydrogenase activity. The larger fragment (Mr = 2 X 37,000) is endowed with full homoserine dehydrogenase activity. These results show that the polypeptide chains of the native enzyme are organized in two different domains, that both domains participate in building up the native dimeric structure, and that one of these domains only is responsible for homoserine dehydrogenase activity. A model of aspartokinase II-homoserine dehydrogenase II is proposed, which accounts for the present results. |
| Links | PubMed |
Significance
You can help EcoliWiki by summarizing why this paper is useful
Useful Materials and Methods
You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.
Annotations
| Gene product | Qualifier | GO ID | GO term name | Evidence Code | with/from | Aspect | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| edit table |
EcoliWiki Links
Add links to pages that link here (e.g. gene, product, method pages)
References
See Help:References for how to manage references in EcoliWiki.