Difference between revisions of "Part:BBa K808013"
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===Usage and Biology=== | ===Usage and Biology=== | ||
− | The monomer of TphA3 consists of 155 amino acids 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 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. |
[[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: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.]]]] | ||
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<partinfo>BBa_K808013 parameters</partinfo> | <partinfo>BBa_K808013 parameters</partinfo> | ||
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==References== | ==References== |
Revision as of 14:32, 25 September 2012
tphA3: Catalyzes together with tphA2 TPA to DCD
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
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.
Sequence and Features
Assembly Compatibility:
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE 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.