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ADARB2  -  adenosine deaminase, RNA-specific, B2 (non...

Homo sapiens

Synonyms: ADAR3, Double-stranded RNA-specific editase B2, RED2, RNA-dependent adenosine deaminase 3, RNA-editing deaminase 2, ...
 
 
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Disease relevance of ADARB2

  • Two ketoreductases, RED1 and RED2, are involved in the biosynthesis of actinorhodin in Streptomyces coelicolor A3(2) and dihydrogranaticin in S. violaceoruber Tu22, respectively [1].
 

High impact information on ADARB2

 

Biological context of ADARB2

 

Associations of ADARB2 with chemical compounds

  • Upon addition of methyl-coenzyme M, the red2 signal disappeared and the red1 signal increased again [5].
  • We report here that in vitro the MCR-red2 state is converted into the MCR-ox1 state by the addition of polysulfide and into a light-sensitive MCR-ox2 state by the addition of sulfite [6].
 

Analytical, diagnostic and therapeutic context of ADARB2

  • Homology modelling studies and site directed mutagenesis showed remarkable differences in three-dimensional structures and catalytic mechanisms between RED1 and RED2 [1].

References

  1. Remarkably different structures and reaction mechanisms of ketoreductases for the opposite stereochemical control in the biosynthesis of BIQ antibiotics. Taguchi, T., Kunieda, K., Takeda-Shitaka, M., Takaya, D., Kawano, N., Kimberley, M.R., Booker-Milburn, K.I., Stephenson, G.R., Umeyama, H., Ebizuka, Y., Ichinose, K. Bioorg. Med. Chem. (2004) [Pubmed]
  2. Requirement of dimerization for RNA editing activity of adenosine deaminases acting on RNA. Cho, D.S., Yang, W., Lee, J.T., Shiekhattar, R., Murray, J.M., Nishikura, K. J. Biol. Chem. (2003) [Pubmed]
  3. A third member of the RNA-specific adenosine deaminase gene family, ADAR3, contains both single- and double-stranded RNA binding domains. Chen, C.X., Cho, D.S., Wang, Q., Lai, F., Carter, K.C., Nishikura, K. RNA (2000) [Pubmed]
  4. Localization of a novel human RNA-editing deaminase (hRED2 or ADARB2) to chromosome 10p15. Mittaz, L., Antonarakis, S.E., Higuchi, M., Scott, H.S. Hum. Genet. (1997) [Pubmed]
  5. The nickel enzyme methyl-coenzyme M reductase from methanogenic archaea: in vitro interconversions among the EPR detectable MCR-red1 and MCR-red2 states. Mahlert, F., Grabarse, W., Kahnt, J., Thauer, R.K., Duin, E.C. J. Biol. Inorg. Chem. (2002) [Pubmed]
  6. The nickel enzyme methyl-coenzyme M reductase from methanogenic archaea: In vitro induction of the nickel-based MCR-ox EPR signals from MCR-red2. Mahlert, F., Bauer, C., Jaun, B., Thauer, R.K., Duin, E.C. J. Biol. Inorg. Chem. (2002) [Pubmed]
 
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