Difference between revisions of "Part:BBa K4515005"
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hbd-opt | hbd-opt | ||
+ | == Profile == | ||
+ | Name: hbd-opt | ||
+ | Base Pairs: 849 bp | ||
+ | |||
+ | Origin: Clostridium acetylbutyrate ATCC824, genome | ||
+ | |||
+ | Properties: β-Hydroxybutyryl-CoA dehydrogenase | ||
+ | == Usage and Biology == | ||
+ | BBa_K4515005 is an enzyme named hbd, which encodes β-Hydroxybutyryl-CoA dehydrogenase and transfers acetoacetyl-CoA into 3- Hydroxybutyryl-CoA in host cells, and plays a key role in the metabolic pathway of N-butanol synthesis [1-2]. It has been found that N-butanol can be synthesized naturally in Clostridium, but the tolerance of Clostridium bacteria is not good enough for large-scale production [3-5]. Recently, Lactobacillus Brevis with better N-butanol tolerance has been isolated by researchers. In order to improve the yield of N-butanol, we optimized the codon of the hbd gene and fused the optimized hbd DNA fragment to the crt-ter DNA fragment with another RBS2 site and co-transcripted (Figure 1), and transformed it into L. brevis ATCC367 competent cells to complete the N-butanol metabolic pathway [6]. | ||
+ | [[File:T--East China--BBa K4515005-Figure1.png|500px|thumb|center|Figure 1. the plasmid map of the composite part BBa_K4515005..]] | ||
+ | ==Reference== | ||
+ | 1.Li, J., Zhao, J. B., Zhao, M., Yang, Y. L., Jiang, W. H., & Yang, S. (2010). Screening and characterization of butanol-tolerant micro-organisms. Letters in applied microbiology, 50(4), 373–379. https://doi.org/10.1111/j.1472-765X.2010.02808.x | ||
+ | |||
+ | 2.Berezina, O. V., Zakharova, N. V., Brandt, A., Yarotsky, S. V., Schwarz, W. H., & Zverlov, V. V. (2010). Reconstructing the clostridial n-butanol metabolic pathway in Lactobacillus brevis. Applied microbiology and biotechnology, 87(2), 635–646. https://doi.org/10.1007/s00253-010-2480-z | ||
+ | |||
+ | 3.Inui M, Suda M, Kimura S, Yasuda K, Suzuki H, Toda H, Yamamoto S, Okino S, Suzuki N, Yukawa H (2008) Expression of Clostridium acetobutylicum butanol synthetic genes in Escherichia coli. Appl Microbiol Biot 77:1305–1316. https://doi.org/10.1007/s00253-007-1257-5 | ||
+ | |||
+ | 4.Mitchell WJ (1998) Physiology of carbohydrate to solvent conversion by Clostridia. In: Poole RK (ed) Advances in Microbial Physiology, vol 39. pp 31–130 | ||
+ | |||
+ | 5.Bowles LK, Ellefson WL (1985) Effects of butanol on Clostridium-acetobutylicum. Appl Environ Microb 50:1165–1170 | ||
+ | |||
+ | 6.Biswas I, Jha JK, Fromm N. (2008) Shuttle expression plasmids for genetic studies in Streptococcus mutans. Microbiology (Reading). Aug;154(Pt 8):2275-2282. doi: 10.1099/mic.0.2008/019265-0. | ||
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Latest revision as of 07:24, 26 September 2022
hbd-opt
hbd-opt
Profile
Name: hbd-opt
Base Pairs: 849 bp
Origin: Clostridium acetylbutyrate ATCC824, genome
Properties: β-Hydroxybutyryl-CoA dehydrogenase
Usage and Biology
BBa_K4515005 is an enzyme named hbd, which encodes β-Hydroxybutyryl-CoA dehydrogenase and transfers acetoacetyl-CoA into 3- Hydroxybutyryl-CoA in host cells, and plays a key role in the metabolic pathway of N-butanol synthesis [1-2]. It has been found that N-butanol can be synthesized naturally in Clostridium, but the tolerance of Clostridium bacteria is not good enough for large-scale production [3-5]. Recently, Lactobacillus Brevis with better N-butanol tolerance has been isolated by researchers. In order to improve the yield of N-butanol, we optimized the codon of the hbd gene and fused the optimized hbd DNA fragment to the crt-ter DNA fragment with another RBS2 site and co-transcripted (Figure 1), and transformed it into L. brevis ATCC367 competent cells to complete the N-butanol metabolic pathway [6].
Reference
1.Li, J., Zhao, J. B., Zhao, M., Yang, Y. L., Jiang, W. H., & Yang, S. (2010). Screening and characterization of butanol-tolerant micro-organisms. Letters in applied microbiology, 50(4), 373–379. https://doi.org/10.1111/j.1472-765X.2010.02808.x
2.Berezina, O. V., Zakharova, N. V., Brandt, A., Yarotsky, S. V., Schwarz, W. H., & Zverlov, V. V. (2010). Reconstructing the clostridial n-butanol metabolic pathway in Lactobacillus brevis. Applied microbiology and biotechnology, 87(2), 635–646. https://doi.org/10.1007/s00253-010-2480-z
3.Inui M, Suda M, Kimura S, Yasuda K, Suzuki H, Toda H, Yamamoto S, Okino S, Suzuki N, Yukawa H (2008) Expression of Clostridium acetobutylicum butanol synthetic genes in Escherichia coli. Appl Microbiol Biot 77:1305–1316. https://doi.org/10.1007/s00253-007-1257-5
4.Mitchell WJ (1998) Physiology of carbohydrate to solvent conversion by Clostridia. In: Poole RK (ed) Advances in Microbial Physiology, vol 39. pp 31–130
5.Bowles LK, Ellefson WL (1985) Effects of butanol on Clostridium-acetobutylicum. Appl Environ Microb 50:1165–1170
6.Biswas I, Jha JK, Fromm N. (2008) Shuttle expression plasmids for genetic studies in Streptococcus mutans. Microbiology (Reading). Aug;154(Pt 8):2275-2282. doi: 10.1099/mic.0.2008/019265-0.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]