Difference between revisions of "Part:BBa K4292009"
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BBa_K4292009 is the coding sequence of E. coli Gmd. The Gmd is made up of 374 aa. Gmd is GDP-D-mannose 4,6-dehydratase. Gmd forms the first step in the biosynthesis of GDP-alpha-D-rhamnose and GDP-alpha-L-fucose [1]. In Aneurinibacillus thermoaerophilus L420-91T, this enzyme acts as a bifunctional enzyme, catalyzing the above reaction as well as the reaction catalyzed by EC 1.1.1.281 [2]. Recently, it has been shown that Gmd have the significant impact in decoration (modification) the main structure of nod factors [3-4]. Protein sequences in the National Center of Biotechnology Information (NCBI) databases showed that GedM are from both prokaryotic and eukaryotic organisms [5]. The recent co-overexpression of gmd, wcaG, manB, and manC contributes to the major flux toward GDP-fucose biosynthesis and a combinatorial modular pathway engineering remarkably enhances the GDP-fucose biosynthesis [6]. | BBa_K4292009 is the coding sequence of E. coli Gmd. The Gmd is made up of 374 aa. Gmd is GDP-D-mannose 4,6-dehydratase. Gmd forms the first step in the biosynthesis of GDP-alpha-D-rhamnose and GDP-alpha-L-fucose [1]. In Aneurinibacillus thermoaerophilus L420-91T, this enzyme acts as a bifunctional enzyme, catalyzing the above reaction as well as the reaction catalyzed by EC 1.1.1.281 [2]. Recently, it has been shown that Gmd have the significant impact in decoration (modification) the main structure of nod factors [3-4]. Protein sequences in the National Center of Biotechnology Information (NCBI) databases showed that GedM are from both prokaryotic and eukaryotic organisms [5]. The recent co-overexpression of gmd, wcaG, manB, and manC contributes to the major flux toward GDP-fucose biosynthesis and a combinatorial modular pathway engineering remarkably enhances the GDP-fucose biosynthesis [6]. | ||
− | [[File:BBa K4292009-figure 1.png|500px|thumb|center| | + | [[File:BBa K4292009-figure 1.png|500px|thumb|center|Figure 1 The reaction catalyzed by Gmd involved in mannose metabolism.]] |
==Reference== | ==Reference== |
Revision as of 07:15, 6 October 2022
E. coli gmd
E. coli gmd
Profile
Name: E. coli gmd
Base Pairs: 1122 bp
Origin: E.coli, genome
Properties: Catalyzes the formation of GDP-4-dehydro-6-deoxy-D-mannose from GDP mannose
Usage and Biology
BBa_K4292009 is the coding sequence of E. coli Gmd. The Gmd is made up of 374 aa. Gmd is GDP-D-mannose 4,6-dehydratase. Gmd forms the first step in the biosynthesis of GDP-alpha-D-rhamnose and GDP-alpha-L-fucose [1]. In Aneurinibacillus thermoaerophilus L420-91T, this enzyme acts as a bifunctional enzyme, catalyzing the above reaction as well as the reaction catalyzed by EC 1.1.1.281 [2]. Recently, it has been shown that Gmd have the significant impact in decoration (modification) the main structure of nod factors [3-4]. Protein sequences in the National Center of Biotechnology Information (NCBI) databases showed that GedM are from both prokaryotic and eukaryotic organisms [5]. The recent co-overexpression of gmd, wcaG, manB, and manC contributes to the major flux toward GDP-fucose biosynthesis and a combinatorial modular pathway engineering remarkably enhances the GDP-fucose biosynthesis [6].
Reference
[1] Kanda Y, Imai-Nishiya H, Kuni-Kamochi R et al (2007) Establishment of a GDP-mannose 4,6-dehydratase (GMD) knockout host cell line: a new strategy for generating completely non-fucosylated recombinant therapeutics. J Biotechnol
[2] Sraphet, S., Javadi, B. (2021) Computational characterizations of GDP-mannose 4,6-dehydratase (NoeL) Rhizobial proteins. Curr Genet 67, 769-784.
[3] Sutherland IW (2001) Microbial polysaccharides from gram-negative bacteria. Int Dairy J 11:663–674
[4]. Szklarczyk D, Gable AL, Lyon D, Junge A, Wyder S, Huerta-Cepas J, Simonovic M, Doncheva NT, Morris JH, Bork P, Jensen LJ, Mering CV (2019) STRING v11: protein-protein association networks with increased coverage, supporting functional discovery in genome-wide experimental datasets. Nucleic Acids Res 47:D607-D613.
[5]. Li W, Zhu Y, Wan L, Guang C, Mu W. (2021) Pathway Optimization of 2'-Fucosyllactose Production in Engineered Escherichia coli. J Agric Food Chem. Feb 10;69(5):1567-1577.
[6] Wan, L.; Zhu, Y.; Li, W.; Zhang, W.; Mu, W. (2020) Combinatorial Modular Pathway Engineering for Guanosine 5′-Diphosphate-l-fucose Production in Recombinant Escherichia coli. J. Agric. Food Chem. 68, 5668-5675.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal AgeI site found at 22
- 1000INCOMPATIBLE WITH RFC[1000]Illegal BsaI site found at 279
Illegal BsaI.rc site found at 439