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Gene Review

HEM3  -  hydroxymethylbilane synthase

Saccharomyces cerevisiae S288c

Synonyms: D1057, HMBS, Hydroxymethylbilane synthase, PBG, Porphobilinogen deaminase, ...
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High impact information on HEM3

  • A hem3 mutant was isolated which was also blocked between 2,3-oxidosqualene and lanosterol (erg12) [1].
  • Analysis of the plasmid designated YEpPBG-D (containing the PBG-D gene) by hybrid-selected translation revealed that it contained the coding information for a single protein of apparent Mr 43,000 [2].
  • The complementing gene restored growth of the hem 3 (PBG-D) mutant strain on media in the absence of exogeneous haem or fatty acid and sterol supplements [2].
  • These findings suggest that HEM3 expression is regulated in the same manner as that of HEM1 which encodes the first enzyme of the heme biosynthetic pathway [3].
  • However, we have found that HAP2 and HAP3 gene products are involved in the expression of HEM3 [3].

Biological context of HEM3


Anatomical context of HEM3

  • Neither LPS nor zymosan increased ROS production by granulocytes incubated in PBG media [5].

Associations of HEM3 with chemical compounds


Analytical, diagnostic and therapeutic context of HEM3

  • Peroxidase activity increased significantly after repeated oral administration of CMG and PBG at doses 150 and 50 mg/kg, SEG 150 mg/kg body mass [8].


  1. 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]
  2. Selection by genetic complementation and characterization of the gene coding for the yeast porphobilinogen deaminase. Gellerfors, P.L., Saltzgaber-Müller, J., Douglas, M.G. Biochem. J. (1986) [Pubmed]
  3. Structure and regulation of yeast HEM3, the gene for porphobilinogen deaminase. Keng, T., Richard, C., Larocque, R. Mol. Gen. Genet. (1992) [Pubmed]
  4. Studies on porphobilinogen-deaminase from Saccharomyces cerevisiae. Correa García, S.R., Rossetti, M.V., Batlle, A.M. Z. Naturforsch., C, J. Biosci. (1991) [Pubmed]
  5. Optimization of conditions for in vitro production of radical oxygen species and expression of tissue factor by canine mononuclear cells and granulocytes for use in high-throughput assays. Okano, S., Hurley, D.J., Bergh, M.S., Vandenplas, M.L., Budsberg, S.C., Moore, J.N. Vet. Immunol. Immunopathol. (2006) [Pubmed]
  6. Yeast porphobilinogen deaminase also forms enzyme-pyrrole intermediates. Correa Garcia, S., Rossetti, M.V., Bermudez Moretti, M., Batlle, A.M. Enzyme Protein (1994) [Pubmed]
  7. Different porphobilinogen-deaminase forms in wild and mutant strains of Saccharomyces cerevisiae. A possible correlation with its segregants behaviour. Correa Garcia, S.R., Rossetti, M.V., Batlle, A.M. Int. J. Biochem. (1991) [Pubmed]
  8. Particulate 1,3-beta-D-glucan, carboxymethylglucan and sulfoethylglucan--influence of their oral or intraperitoneal administration on immunological respondence of mice. Mucksová, J., Babícek, K., Pospísil, M. Folia Microbiol. (Praha) (2001) [Pubmed]
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