Difference between revisions of "YJR139C"
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− | '''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='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|S000056674}} PMID 1897932 | + | '''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|S000056674}} PMID 1897932</ref> | |
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Revision as of 14:05, 25 February 2010
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Systematic name | YJR139C |
Gene name | HOM6 |
Aliases | |
Feature type | ORF, Verified |
Coordinates | Chr X:690514..689435 |
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]
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References
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- ↑ 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
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