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LEU1 protein (Saccharomyces cerevisiae) - STRING interaction network
"LEU1" - Isopropylmalate isomerase, catalyzes the second step in the leucine biosynthesis pathway in Saccharomyces cerevisiae
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Predicted Interactions
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LEU1Isopropylmalate isomerase, catalyzes the second step in the leucine biosynthesis pathway; Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate (779 aa)    
Predicted Functional Partners:
LEU2
Beta-isopropylmalate dehydrogenase (IMDH), catalyzes the third step in the leucine biosynthesis pathway; Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate (364 aa)
 
  0.999
LEU4
Alpha-isopropylmalate synthase (2-isopropylmalate synthase); the main isozyme responsible for the first step in the leucine biosynthesis pathway; Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate) (619 aa)
   
  0.999
LEU9
Alpha-isopropylmalate synthase II (2-isopropylmalate synthase), catalyzes the first step in the leucine biosynthesis pathway; the minor isozyme, responsible for the residual alpha-IPMS activity detected in a leu4 null mutant; Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate). Redundant to LEU4, responsible of about 20% of alpha-IPMS activity. Involved in leucine synthesis (604 aa)
   
  0.999
IDH2
Subunit of mitochondrial NAD(+)-dependent isocitrate dehydrogenase, which catalyzes the oxidation of isocitrate to alpha-ketoglutarate in the TCA cycle; phosphorylated; Performs an essential role in the oxidative function of the citric acid cycle. Also binds RNA; specifically to the 5’- untranslated leaders of mitochondrial mRNAs (369 aa)
   
  0.999
IDH1
Subunit of mitochondrial NAD(+)-dependent isocitrate dehydrogenase, which catalyzes the oxidation of isocitrate to alpha-ketoglutarate in the TCA cycle; Performs an essential role in the oxidative function of the citric acid cycle. Also binds RNA; specifically to the 5’- untranslated leaders of mitochondrial mRNAs (360 aa)
   
  0.998
LYS12
Homo-isocitrate dehydrogenase, an NAD-linked mitochondrial enzyme required for the fourth step in the biosynthesis of lysine, in which homo-isocitrate is oxidatively decarboxylated to alpha-ketoadipate; Catalyzes the NAD(+)-dependent conversion of homoisocitrate to alpha-ketoadipate (371 aa)
   
  0.998
LYS21
Homocitrate synthase isozyme, catalyzes the condensation of acetyl-CoA and alpha-ketoglutarate to form homocitrate, which is the first step in the lysine biosynthesis pathway; highly similar to the other isozyme, Lys20p (440 aa)
 
  0.995
LYS20
Homocitrate synthase isozyme, catalyzes the condensation of acetyl-CoA and alpha-ketoglutarate to form homocitrate, which is the first step in the lysine biosynthesis pathway; highly similar to the other isozyme, Lys21p (428 aa)
 
  0.992
GLT1
NAD(+)-dependent glutamate synthase (GOGAT), synthesizes glutamate from glutamine and alpha-ketoglutarate; with Gln1p, forms the secondary pathway for glutamate biosynthesis from ammonia; expression regulated by nitrogen source; Forms L-glutamate from L-glutamine and 2-oxoglutarate. Represents an alternative pathway to L-glutamate dehydrogenase for the biosynthesis of L-glutamate. Participates with glutamine synthetase in ammonia assimilation processes. The enzyme is specific for NADH, L-glutamine and 2-oxoglutarate (2145 aa)
   
 
  0.988
BAT1
Mitochondrial branched-chain amino acid (BCAA) aminotransferase, preferentially involved in BCAA biosynthesis; homolog of murine ECA39; highly expressed during logarithmic phase and repressed during stationary phase; Involved in the biosynthesis of the branched chain amino acids leucine, isoleucine, and valine. Catalyzes the formation of methionine from 2-keto-4-methylthiobutyrate (KMTB) in the methionine salvage pathway primarily using branched chain amino acids (leucine, isoleucine, and valine) as the amino donors. Appears to be involved in the regulation of the transition from G1 to [...] (393 aa)
   
   
  0.988
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: Candida robusta, Pachytichospora, S. cerevisiae, Saccharomyces, Saccharomyces capensis, Saccharomyces cerevisiae, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, lager beer yeast, yeast
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