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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
Gene Review

hmpA  -  nitric oxide dioxygenase

Escherichia coli CFT073

 
 
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Disease relevance of hmpA

  • The NMR data revealed differences in the intracellular carbon fluxes between E. coli cells expressing either VHb or VHb-Red and cells expressing A. eutrophus FHP or the truncated heme domain (FHPg) [1].
  • The amino-terminal hemoglobin domain of the flavohemoprotein (FHP) of the gram-negative hydrogen-oxidizing bacterium Alcaligenes eutrophus has 51% sequence homology with VHb [2].
  • Engineering, expression and biochemical characterization of the hemoglobin domain of a Erwinia chrysanthemi flavohemoprotein [3].
  • In this study we constructed an artificial flavohemoprotein by fusing Vitreoscilla hemoglobin (VHb) with D-amino acid oxidase (DAO) of Rhodotorula gracilis to determine whether bacterial hemoglobin can be used as an oxygen donor to immobilized flavoenzyme [4].
 

High impact information on hmpA

  • Consistently, E. coli cells displaying FHP and FHPg activity showed lower production of the typical anaerobic by-products formate, acetate, and D-lactate [1].
  • The presence of FHP or of VHb-FAD-NAD reductase increased the final cell density of transformed wild-type E. coli cells approximately 50 and 75%, respectively, for hypoxic fed-batch culture relative to the control synthesizing VHb [2].
  • When the resting flavohemoprotein was aerobically incubated with NAD(P)H, it was converted to a spectral species that is spectrally very similar to oxyhemoglobins [5].

References

  1. Dissection of central carbon metabolism of hemoglobin-expressing Escherichia coli by 13C nuclear magnetic resonance flux distribution analysis in microaerobic bioprocesses. Frey, A.D., Fiaux, J., Szyperski, T., Wüthrich, K., Bailey, J.E., Kallio, P.T. Appl. Environ. Microbiol. (2001) [Pubmed]
  2. Expression of Alcaligenes eutrophus flavohemoprotein and engineered Vitreoscilla hemoglobin-reductase fusion protein for improved hypoxic growth of Escherichia coli. Frey, A.D., Bailey, J.E., Kallio, P.T. Appl. Environ. Microbiol. (2000) [Pubmed]
  3. Engineering, expression and biochemical characterization of the hemoglobin domain of a Erwinia chrysanthemi flavohemoprotein. Labesse, G., Craescu, C.T., Mispelter, J., Chottard, G., Marden, M.C., Pin, S., Forest, E., Mornon, J.P., Boccara, M. Eur. J. Biochem. (1998) [Pubmed]
  4. Fusion protein of Vitreoscilla hemoglobin with D-amino acid oxidase enhances activity and stability of biocatalyst in the bioconversion process of cephalosporin C. Khang, Y.H., Kim, I.W., Hah, Y.R., Hwangbo, J.H., Kang, K.K. Biotechnol. Bioeng. (2003) [Pubmed]
  5. Purification and characterization of a flavohemoglobin from the denitrifying fungus Fusarium oxysporum. Takaya, N., Suzuki, S., Matsuo, M., Shoun, H. FEBS Lett. (1997) [Pubmed]
 
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