glgCAB for polycistronic expression of glycogen synthesis genes in E.coli
This composite part combines all 3 enzymes enzymes involved in glycogen synthesis. GlgC creates ADP-glucose from glucose-1-phosphate, GlgA elongates alpha-1,4-linked chains and GlgB catalyzes the formation of alpha-1,6-linked branches.
Sarah Lubjuhn, Laura Helleckes, Michael Osthege
This is the translational unit of GlgB (glycogen branching enzyme) from E. coli. The enzyme catalyzes the formation of alpha-1,6-branches in glycogen synthesis.
This is the translational unit of GlgA (Glycogen synthase) for elongation of glycogen chains. Through autophosphorylation, GlgA is also the starting point of glycogen synthesis in bacteria.
Laura Helleckes, Michael Osthege, Sarah Lubjuhn
This is the translational unit of GlgC. It creates ADP-glucose from glucose-1-phosphate for glycogen synthesis.
Michael Osthege, Sarah Lubjuhn, Laura Helleckes
The BioBrick was created from the genomic sequence of glgA in ''E. coli'' K12.
The glycogen synthase synthesizes alpha-1,4-glucan chains using ADP-glucose. The BioBrick was created from the genomic sequence of glgA in ''E. coli'' K12. Six illegal restriction sites were removed to ensure full BioBrick compability.
Six illegal restriction sites were removed to ensure full BioBrick compability. The native stop codon was replaced with TAATAA.
branching enzyme; synthesizes branches in glycogen; from E.coli
RBS (Elowitz 1999) -- defines RBS efficiency
Varies from -6 to +1 region from original sequence to accomodate BioBricks suffix. No secondary structures are formed in the given RBS region. Users should check for secondary structures induced in the RBS by upstream and downstream elements in the +50 to -50 region, as such structures will greatly affect the strength of the RBS. Contact info for this part: Brian Chow
Vinay S Mahajan, Voichita D. Marinescu, Brian Chow, Alexander D Wissner-Gross and Peter Carr IAP, 2003.
This is the coding sequence of ''glgC'' (ADP-glucose pyrophosphorylase) from ''Escherichia coli'' JM109 with the substitution G336D. This mutation is known to cause increased activity of ADP-glucose pyrophosphorylase in the absence of the activator fructose 1,6-bisphosphate (FBP), high affinity for FBP and substrates lower affinity for the inhibitor AMP. (Leung ''et al'', 1986; Meyer ''et al.'', 1988)
The mutation G336D was achieved by the substitution of A for G at position 1076 (codon GGC->GAC) by MABEL.
Conversion of the iGEM parts registry to SBOL2.1