Difference between revisions of "Part:BBa K808013"
(→‎Usage and Biology)
 
(2 intermediate revisions by 2 users not shown)
Line 4: Line 4:
 
[[Image:Tph3.png.png|300px|thumb|right|Figure 1. '''Homology modelling of TphA3'''. For simulation parameters [[http://2012.igem.org/Team:TU_Darmstadt/Modeling_Homologie_Modeling#TphA3 click here.]]]]
 
[[Image:Tph3.png.png|300px|thumb|right|Figure 1. '''Homology modelling of TphA3'''. For simulation parameters [[http://2012.igem.org/Team:TU_Darmstadt/Modeling_Homologie_Modeling#TphA3 click here.]]]]
  
−
''TphA3'' is coding for the small terephthalate 1,2-dioxygenase subunit from ''Comamonas testosteroni KF-1''. TphA3 forms together with TphA1 and TphA2 the terephthalic acid 1,2-dioxigenase system (TERDOS). TERDOS catalyzes the first reaction in the terephthalic acid degradation
+
''TphA3'' is coding for the small terephthalate 1,2-dioxygenase subunit from ''Comamonas testosteroni KF-1''. TphA3 forms together with TphA1 and TphA2 the terephthalic acid 1,2-dioxygenase system (TERDOS). TERDOS catalyzes the first reaction in the terephthalic acid degradation
  
  
Line 12: Line 12:
 
===Usage and Biology===
 
===Usage and Biology===
  
−
The monomer of TphA3 consists of 155 amino acids and a molar mass of 17.36 kDa.By gel permeation chromatography, we could show that TphA3 has a homotrimeric structure and a mass of 52.08 kDa.
+
The monomer of TphA3 consists of 155 amino acids and has a molar mass of 17.36 kDa. Gel permeation chromatography shows that TphA3 has a homotrimeric structure and a mass of 52.08 kDa.
  
−
[[Image:GPC_tphA3.jpg|550px|thumb|left|Figure 2. '''GPC analysis of TphA3'''. The Peak of TphA3 has a retention time of 33 minutes. This retention time equates a molar mass of 52 kDa, approximately.[[http://2012.igem.org/Team:TU_Darmstadt/Modeling_Homologie_Modeling#TphA3 click here.]]]]
+
[[Image:TphA3.JPG|550px|thumb|left|Figure 2. '''GPC analysis of TphA3'''. The Peak of TphA3 has a retention time of 33 minutes. This retention time equates a molar mass of 52 kDa, approximately.[[http://2012.igem.org/Team:TU_Darmstadt/Labjournal/Metabolism#Gel_permeation_chromatography click here.]]]]
  
  

Latest revision as of 01:01, 27 September 2012

tphA3: Catalyzes together with tphA2 TPA to DCD

Figure 1. Homology modelling of TphA3. For simulation parameters http://2012.igem.org/Team:TU_Darmstadt/Modeling_Homologie_Modeling#TphA3 click here.

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



Usage and Biology

The monomer of TphA3 consists of 155 amino acids and has a molar mass of 17.36 kDa. Gel permeation chromatography shows that TphA3 has a homotrimeric structure and a mass of 52.08 kDa.

Figure 2. GPC analysis of TphA3. The Peak of TphA3 has a retention time of 33 minutes. This retention time equates a molar mass of 52 kDa, approximately.http://2012.igem.org/Team:TU_Darmstadt/Labjournal/Metabolism#Gel_permeation_chromatography click here.











Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 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.