Difference between revisions of "Part:BBa K808011"

(→‎Usage and Biology)
Line 4: Line 4:
 
[[Image:TPHA1.full.png|300px|thumb|right|Figure 1. '''Homology modelling of TphA1'''. For simulation parameters [[http://2012.igem.org/Team:TU_Darmstadt/Modeling_Homologie_Modeling#TphA1 click here.]]]]
 
[[Image:TPHA1.full.png|300px|thumb|right|Figure 1. '''Homology modelling of TphA1'''. For simulation parameters [[http://2012.igem.org/Team:TU_Darmstadt/Modeling_Homologie_Modeling#TphA1 click here.]]]]
  
−
TphA1 is coding for the terephthalate dioxygenase reductase from ''Comamonas testosteroni KF-1''. TphA1 forms together with tphA2 and tphA3 the terephthalic acid 1,2-dioxigenase system (TERDOS). TERDOS catalyzes the first reaction in the terephthalic acid degradation.
+
TphA1 is coding for the terephthalate dioxygenase reductase from ''Comamonas testosteroni KF-1''. TphA1 forms together with TphA2 and TphA3 the terephthalic acid 1,2-dioxygenase system (TERDOS). TERDOS catalyzes the first reaction in the terephthalic acid degradation.
  
  
Line 11: Line 11:
 
===Usage and Biology===
 
===Usage and Biology===
  
−
TphA1 is just like TphA2 an Rieske protein with an iron-sulfur center. In addition to the Rieske center, TphA1 has a binding site for NADPH + H<sup>+</sup>. The catalytic domain oxidizes NADPH + H<sup>+</sup> and reduces TphA1. Afterwards the reduced TphA1 reduces the TphA2A3 complex.
+
TphA1 is just like TphA2 an Rieske protein with an iron-sulfur center. In addition to the Rieske center, TphA1 has a binding site for NADPH + H<sup>+</sup>. The catalytic domain oxidizes NADPH + H<sup>+</sup> and reduces TphA1. Afterwards the reduced TphA1 reduces the TphA2A3 complex and is again in the oxidized state.
  
  

Revision as of 19:33, 25 September 2012

tphA1: reduces the tphA2A3 complex

Figure 1. Homology modelling of TphA1. For simulation parameters http://2012.igem.org/Team:TU_Darmstadt/Modeling_Homologie_Modeling#TphA1 click here.

TphA1 is coding for the terephthalate dioxygenase reductase from Comamonas testosteroni KF-1. TphA1 forms together with TphA2 and TphA3 the terephthalic acid 1,2-dioxygenase system (TERDOS). TERDOS catalyzes the first reaction in the terephthalic acid degradation.



Usage and Biology

TphA1 is just like TphA2 an Rieske protein with an iron-sulfur center. In addition to the Rieske center, TphA1 has a binding site for NADPH + H+. The catalytic domain oxidizes NADPH + H+ and reduces TphA1. Afterwards the reduced TphA1 reduces the TphA2A3 complex and is again in the oxidized state.









Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    INCOMPATIBLE WITH RFC[12]
    Illegal NheI site found at 954
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal NgoMIV site found at 85
    Illegal NgoMIV site found at 394
  • 1000
    COMPATIBLE WITH RFC[1000]


References

  • Sasoh, M., E. Masai, et al. (2006). "Characterization of the terephthalate degradation genes of Comamonas sp. strain E6." Appl Environ Microbiol 72(3): 1825-1832.
  • Fukuhara, Y., K. Inakazu, et al. (2010). "Characterization of the isophthalate degradation genes of Comamonas sp. strain E6." Appl Environ Microbiol 76(2): 519-527.
  • Kamimura, N., T. Aoyama, et al. (2010). "Characterization of the protocatechuate 4,5-cleavage pathway operon in Comamonas sp. strain E6 and discovery of a novel pathway gene." Appl Environ Microbiol 76(24): 8093-8101.
  • Schläfli HR, Weiss MA, Leisinger T, Cook AM. (1994)"Terephthalate 1,2-dioxygenase system from Comamonas testosteroni T-2: purification and some properties of the oxygenase component." J Bacteriol. 1994 Nov;176(21):6644-52.