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Gene Review:

hemA - glutamyl-tRNA reductase

Escherichia coli CFT073

Qin, G. et al., Choi, H.P. et al., Gase, K. et al.

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Disease relevance of hemA

However, unlike the hel gene, lppC was unable to complement hemA mutants of E. coli for growth on hemin as sole porphyrin source in aerobic conditions [1].
The hemA gene encoding 5-aminolevulinic acid synthase (ALAS) was cloned from the genomic DNA of photosynthetic bacterium Rhodopseudomonas palustris KUGB306 [2].

High impact information on hemA

The recombinant Escherichia coli BL21(DE3) harboring hemA from Agrobacterium radiobacter, which was engineered in our previous work, was used for the extracellular production of 5-aminolevulinic acid (ALA) [3].

References

The lppC gene of Streptococcus equisimilis encodes a lipoprotein that is homologous to the e (P4) outer membrane protein from Haemophilus influenzae. Gase, K., Liu, G., Bruckmann, A., Steiner, K., Ozegowski, J., Malke, H. Med. Microbiol. Immunol. (Berl.) (1997) [Pubmed]
Cloning, expression, and characterization of 5-aminolevulinic acid synthase from Rhodopseudomonas palustris KUGB306. Choi, H.P., Hong, J.W., Rhee, K.H., Sung, H.C. FEMS Microbiol. Lett. (2004) [Pubmed]
Effects of medium composition on production of 5-aminolevulinic acid by recombinant Escherichia coli. Qin, G., Lin, J., Liu, X., Cen, P. J. Biosci. Bioeng. (2006) [Pubmed]

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