Difference between revisions of "Part:BBa K808012"
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===Usage and Biology===
 
===Usage and Biology===
  
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TphA2 consists of 414 amino acids and has a molar mass of 46.35 kDa. It is Rieske protein with a iron-sulfuric center. The Rieske center is located in the active site and is typical for oxygenases. Figure 1 shows TphA1 with the Rieske center.
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TphA2 consists of 414 amino acids and has a molar mass of 46.35 kDa. It is a Rieske protein with a iron-sulfuric center. The Rieske center is located in the active site and is typical for oxygenases. Figure 1 shows TphA1 with the Rieske center.
  
  
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<span class='h3bb'>Sequence and Features</span>
 
<span class='h3bb'>Sequence and Features</span>
 
<partinfo>BBa_K808012 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K808012 SequenceAndFeatures</partinfo>
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==References==
 
==References==

Revision as of 19:40, 25 September 2012

tphA2: Catalyzes together with tphA3 TPA to DCD

Figure 1. Homology modelling of TphA2. For simulation parameters http://2012.igem.org/Team:TU_Darmstadt/Modeling_Homologie_Modeling#TphA3 click here.

tphA2 is coding for the lagre terephthalate 1,2-dioxygenase subunit from Comamonas testosteroni KF-1. TphA2 forms together with TphA1 and TphA3 the terephthalic acid 1,2-dioxygenase system (TERDOS). TERDOS catalyzes the first reaction in the terephthalic acid degradation.


Usage and Biology

TphA2 consists of 414 amino acids and has a molar mass of 46.35 kDa. It is a Rieske protein with a iron-sulfuric center. The Rieske center is located in the active site and is typical for oxygenases. Figure 1 shows TphA1 with the Rieske center.









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
    INCOMPATIBLE WITH RFC[25]
    Illegal NgoMIV site found at 390
  • 1000
    INCOMPATIBLE WITH RFC[1000]
    Illegal SapI.rc site found at 409

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.