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Gene Review

HOM3  -  aspartate kinase

Saccharomyces cerevisiae S288c

Synonyms: Aspartate kinase, Aspartokinase, BOR1, SIL4, THR3, ...
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Disease relevance of HOM3


High impact information on HOM3


Chemical compound and disease context of HOM3


Biological context of HOM3


Anatomical context of HOM3

  • Bor1p, the yeast band 3 homolog, localizes to the vacuole [5].

Associations of HOM3 with chemical compounds


Regulatory relationships of HOM3

  • All 8 induced 2-5-fold increases in reversion frequencies over background at the trp5 locus--5 of these induced 1.5-3-fold increases at the hom3 locus and 1 induced a doubling at his1 [11].

Other interactions of HOM3

  • Transcriptional and biochemical regulation of a novel Arabidopsis thaliana bifunctional aspartate kinase-homoserine dehydrogenase gene isolated by functional complementation of a yeast hom6 mutant [10].
  • In a BOR3 mutant, THR1, HOM2 and HOM3 mRNA levels were increased slightly [12].
  • A sequence comparison among all the reported mutant aspartate kinases suggests that not all residues involved in regulation of the activity are clustered in the so-called regulatory domain, as is the case of that mutated in AK-R7, another deregulated aspartate kinase obtained with the same strategy of ilv1 suppression [8].

Analytical, diagnostic and therapeutic context of HOM3

  • Gel filtration and native gel electrophoresis indicated that yeast AK is a homohexamer of 346 kDa composed by 58 kDa subunits [13].


  1. Structure of the yeast HOM3 gene which encodes aspartokinase. Rafalski, J.A., Falco, S.C. J. Biol. Chem. (1988) [Pubmed]
  2. Aspartate kinase-independent lysine synthesis in an extremely thermophilic bacterium, Thermus thermophilus: lysine is synthesized via alpha-aminoadipic acid not via diaminopimelic acid. Kobashi, N., Nishiyama, M., Tanokura, M. J. Bacteriol. (1999) [Pubmed]
  3. FKBP12 physically and functionally interacts with aspartokinase in Saccharomyces cerevisiae. Alarcón, C.M., Heitman, J. Mol. Cell. Biol. (1997) [Pubmed]
  4. Genetic and biochemical study of threonine-overproducing mutants of Saccharomyces cerevisiae. Delgado, M.A., Guerrero, J., Conde, J. Mol. Cell. Biol. (1982) [Pubmed]
  5. Enolase activates homotypic vacuole fusion and protein transport to the vacuole in yeast. Decker, B.L., Wickner, W.T. J. Biol. Chem. (2006) [Pubmed]
  6. Mutations that cause threonine sensitivity identify catalytic and regulatory regions of the aspartate kinase of Saccharomyces cerevisiae. Arévalo-Rodríguez, M., Calderón, I.L., Holmberg, S. Yeast (1999) [Pubmed]
  7. Molecular analysis of the aspartate kinase-homoserine dehydrogenase gene from Arabidopsis thaliana. Ghislain, M., Frankard, V., Vandenbossche, D., Matthews, B.F., Jacobs, M. Plant Mol. Biol. (1994) [Pubmed]
  8. A new mutation in the yeast aspartate kinase induces threonine accumulation in a temperature-regulated way. Velasco, I., Arévalo-Rodríguez, M., Marina, P., Calderón, I.L. Yeast (2005) [Pubmed]
  9. Genetics of borrelidin resistant mutants of Saccharomyces cerivisiae and properties of their threonyl-tRNA-synthetase. Nass, G., Poralla, K. Mol. Gen. Genet. (1976) [Pubmed]
  10. Transcriptional and biochemical regulation of a novel Arabidopsis thaliana bifunctional aspartate kinase-homoserine dehydrogenase gene isolated by functional complementation of a yeast hom6 mutant. Rognes, S.E., Dewaele, E., Aas, S.F., Jacobs, M., Frankard, V. Plant Mol. Biol. (2003) [Pubmed]
  11. Mutagenicity of constituents of pulp and paper mill effluent in growing cells of Saccharomyces cerevisiae. Nestmann, E.R., Lee, E.G. Mutat. Res. (1983) [Pubmed]
  12. Four major transcriptional responses in the methionine/threonine biosynthetic pathway of Saccharomyces cerevisiae. Mountain, H.A., Byström, A.S., Larsen, J.T., Korch, C. Yeast (1991) [Pubmed]
  13. Characterization of the aspartate kinase from Saccharomyces cerevisiae and of its interaction with threonine. Marina, P., Martínez-Costa, O.H., Calderón, I.L., Aragón, J.J. Biochem. Biophys. Res. Commun. (2004) [Pubmed]
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