Difference between revisions of "YJR139C"
SGDwikiBot (talk | contribs) (Automated import of articles) |
SGDwikiBot (talk | contribs) (Automated import of articles) |
||
| (9 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
<!-- PLEASE DO NOT EDIT HERE. USE THE SECTION EDIT LINKS ON THE RIGHT MARGIN--> | <!-- PLEASE DO NOT EDIT HERE. USE THE SECTION EDIT LINKS ON THE RIGHT MARGIN--> | ||
{{PageTop}} | {{PageTop}} | ||
| + | <protect> | ||
{|{{Prettytable}} align = 'right' width = '200px' | {|{{Prettytable}} align = 'right' width = '200px' | ||
|- | |- | ||
| − | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http:// | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000003900 YJR139C] |
|- | |- | ||
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''HOM6 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''HOM6 '' | ||
|- | |- | ||
| − | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Aliases''' ||'' '' | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Aliases''' ||''THR6'' |
|- | |- | ||
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Feature type''' || ORF, Verified[[Category:ORF]][[Category:ORF, Verified]] | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Feature type''' || ORF, Verified[[Category:ORF]][[Category:ORF, Verified]] | ||
|- | |- | ||
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
| − | |nowrap| Chr X: | + | |nowrap| Chr X:690524..689445 |
|- | |- | ||
| − | | | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000003900 |
|} | |} | ||
<br> | <br> | ||
| − | '''Description of | + | '''Description of YJR139C:''' Homoserine dehydrogenase (L-homoserine:NADP oxidoreductase), dimeric enzyme that catalyzes the third step in the common pathway for methionine and threonine biosynthesis; enzyme has nucleotide-binding, dimerization and catalytic regions<ref name='S000063546'>DeLaBarre B, et al. (2000) Crystal structures of homoserine dehydrogenase suggest a novel catalytic mechanism for oxidoreductases. Nat Struct Biol 7(3):238-44 {{SGDpaper|S000063546}} PMID 10700284</ref><ref name='S000040395'>Thomas D, et al. (1993) Evolutionary relationships between yeast and bacterial homoserine dehydrogenases. FEBS Lett 323(3):289-93 {{SGDpaper|S000040395}} PMID 8500624</ref><ref name='S000056674'>Yumoto N, et al. (1991) Rapid purification and characterization of homoserine dehydrogenase from Saccharomyces cerevisiae. Arch Biochem Biophys 285(2):270-5 |
| − | {{SGDpaper| | + | {{SGDpaper|S000056674}} PMID 1897932</ref> |
<br> | <br> | ||
<br> | <br> | ||
<br> | <br> | ||
<br> | <br> | ||
| − | + | <br> | |
| + | </protect> | ||
__TOC__ | __TOC__ | ||
==Community Commentary== | ==Community Commentary== | ||
{{CommentaryHelp}} | {{CommentaryHelp}} | ||
| + | |||
| + | |||
| + | |||
| + | <!-- PLEASE ADD Community Commentary ABOVE THIS MESSAGE. See below for an example of community annotation --> | ||
| + | <!-- | ||
| + | Specifically higher expression in carbon limited chemostat cultures versus carbon excess. | ||
| + | <ref>Boer VM, et al. (2003) The genome-wide transcriptional responses of Saccharomyces cerevisiae grown on glucose in aerobic chemostat cultures limited for carbon, nitrogen, phosphorus, or sulfur. | ||
| + | J Biol Chem 278(5):3265-74</ref> | ||
| + | --> | ||
| + | |||
| + | |||
| + | |||
| + | <protect> | ||
==References== | ==References== | ||
<!-- REFERENCES ARE AUTOMATICALLY GENERATED. PLEASE DON'T EDIT THIS SECTION--> | <!-- REFERENCES ARE AUTOMATICALLY GENERATED. PLEASE DON'T EDIT THIS SECTION--> | ||
{{RefHelp}} | {{RefHelp}} | ||
| + | </protect> | ||
Latest revision as of 14:05, 14 May 2012
Share your knowledge...Edit this entry! <protect>
| Systematic name | YJR139C |
| Gene name | HOM6 |
| Aliases | THR6 |
| Feature type | ORF, Verified |
| Coordinates | Chr X:690524..689445 |
| Primary SGDID | S000003900 |
Description of YJR139C: Homoserine dehydrogenase (L-homoserine:NADP oxidoreductase), dimeric enzyme that catalyzes the third step in the common pathway for methionine and threonine biosynthesis; enzyme has nucleotide-binding, dimerization and catalytic regions[1][2][3]
</protect>
Contents
Community Commentary
About Community Commentary. Please share your knowledge!
<protect>
References
See Help:References on how to add references
- ↑ DeLaBarre B, et al. (2000) Crystal structures of homoserine dehydrogenase suggest a novel catalytic mechanism for oxidoreductases. Nat Struct Biol 7(3):238-44 SGD PMID 10700284
- ↑ Thomas D, et al. (1993) Evolutionary relationships between yeast and bacterial homoserine dehydrogenases. FEBS Lett 323(3):289-93 SGD PMID 8500624
- ↑ Yumoto N, et al. (1991) Rapid purification and characterization of homoserine dehydrogenase from Saccharomyces cerevisiae. Arch Biochem Biophys 285(2):270-5 SGD PMID 1897932
See Help:Categories on how to add the wiki page for this gene to a Category </protect>
