Difference between revisions of "Part:BBa K4292009"

 
 
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== Profile ==
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===Usage and Biology===
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Name: E. coli gmd
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Base Pairs: 1122 bp
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Origin: E.coli, genome
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Properties: Catalyzes the formation of GDP-4-dehydro-6-deoxy-D-mannose from GDP mannose
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== Usage and Biology ==
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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].
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[[File:BBa K4292009-figure 1.png|500px|thumb|center|Figure 1. The reaction catalyzed by Gmd involved in mannose metabolism.]]
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==Reference==
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[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
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[2] Sraphet, S., Javadi, B. (2021) Computational characterizations of GDP-mannose 4,6-dehydratase (NoeL) Rhizobial proteins. Curr Genet 67, 769-784.
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[3] Sutherland IW (2001) Microbial polysaccharides from gram-negative bacteria. Int Dairy J 11:663–674
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[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.
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[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.
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[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.
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Latest revision as of 07:16, 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].

Figure 1. The reaction catalyzed by Gmd involved in mannose metabolism.

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


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 AgeI site found at 22
  • 1000
    INCOMPATIBLE WITH RFC[1000]
    Illegal BsaI site found at 279
    Illegal BsaI.rc site found at 439