The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

HEM2  -  porphobilinogen synthase HEM2

Saccharomyces cerevisiae S288c

Synonyms: ALADH, Delta-aminolevulinic acid dehydratase, OLE4, Porphobilinogen synthase, SLU1, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of HEM2

  • The crystal structure of the Mg2+-dependent PBGS from the human pathogen Pseudomonas aeruginosa in complex with the competitive inhibitor levulinic acid (LA) solved at 1.67 A resolution shows a homooctameric enzyme that consists of four asymmetric dimers [1].

High impact information on HEM2

  • These mutations are leaky versions of HEM2 and HEM4, respectively; addition of exogenous hemin reverses the suppressing effects of slu1 and slu2 [2].
  • Characterization of the yeast HEM2 gene and transcriptional regulation of COX5 and COR1 by heme [3].
  • A gene capable of complementing the respiratory deficiency of C41 and N28 has been cloned by transformation of a hem2 mutant with a recombinant plasmid library of wild type yeast nuclear DNA [3].
  • The mutants are unable to convert delta-aminolevulinic acid to porphobilinogen and are not complemented by the hem2 mutant GL4 (Gollub, E. G., Liu, K.-P., Dagan, J., Adlersberg, M., and Sprinson, D. B. (1977) J. Biol. Chem. 252, 2846-2854) [3].
  • Mutants in hem1, hem2, and hem3 had an additional requirement for methionine on synthetic medium supplemented with either heme or ergosterol and Tween 80, owing to a lack of sulfite reductase which contains siroheme, a modified uroporphyrin III [4].

Biological context of HEM2


Associations of HEM2 with chemical compounds


  1. High resolution crystal structure of a Mg2+-dependent porphobilinogen synthase. Frankenberg, N., Erskine, P.T., Cooper, J.B., Shoolingin-Jordan, P.M., Jahn, D., Heinz, D.W. J. Mol. Biol. (1999) [Pubmed]
  2. A yeast sterol auxotroph (erg25) is rescued by addition of azole antifungals and reduced levels of heme. Gachotte, D., Pierson, C.A., Lees, N.D., Barbuch, R., Koegel, C., Bard, M. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  3. Characterization of the yeast HEM2 gene and transcriptional regulation of COX5 and COR1 by heme. Myers, A.M., Crivellone, M.D., Koerner, T.J., Tzagoloff, A. J. Biol. Chem. (1987) [Pubmed]
  4. Yeast mutants deficient in heme biosynthesis and a heme mutant additionally blocked in cyclization of 2,3-oxidosqualene. Gollub, E.G., Liu, K.P., Dayan, J., Adlersberg, M., Sprinson, D.B. J. Biol. Chem. (1977) [Pubmed]
  5. Purification of delta-aminolevulinate dehydratase from genetically engineered yeast. Borralho, L.M., Ortiz, C.H., Panek, A.D., Mattoon, J.R. Yeast (1990) [Pubmed]
  6. A role for HEM2 in cadmium tolerance. Hunter, T.C., Mehra, R.K. J. Inorg. Biochem. (1998) [Pubmed]
  7. Heterologous expression of human 5-aminolevulinate dehydratase in Saccharomyces cerevisiae. Schauer, W.E., Mattoon, J.R. Curr. Genet. (1990) [Pubmed]
  8. Modulation of cytochrome biosynthesis in yeast by antimetabolite action of levulinic acid. Malamud, D.R., Borralho, L.M., Panek, A.D., Mattoon, J.R. J. Bacteriol. (1979) [Pubmed]
WikiGenes - Universities