GlgX (EC 3.2.1.196) is a limit dextrin α-1,6-maltotetraose-hydrolase that selectively hydrolyzes α-1,6-glycosidic linkages in phosphorylase-limit dextrins with branches of three or four glucose residues . Unlike eukaryotic debranching enzymes, GlgX does not require a separate 4-α-glucanotransferase, enabling direct debranching of short outer chains during glycogen breakdown .
The glgX gene is part of the glgBXCAP operon, which coordinates glycogen synthesis and degradation . Disruption of glgX leads to:
Glycogen overproduction: Mutants (ΔglgX) accumulate glycogen with altered chain-length distributions .
Structural abnormalities: Increased proportions of very short (4–6 DP) and long (≥17 DP) chains compared to wild-type glycogen .
Studies in E. coli K12 mutants reveal:
Growth enhancement: ΔglgX strains show higher OD600 at stationary phase compared to wild-type .
Environmental stress responses:
While no direct studies on E. coli O9:H4 GlgX exist, recombinant forms are inferred from conserved mechanisms:
| Strain | Glycogen Content (μg/mg) | Average Chain Length (DP) | Phenotype |
|---|---|---|---|
| Wild-type | 12.5 ± 1.2 | 12.04 ± 0.28 | Normal growth, iodine+ |
| ΔglgX | 28.7 ± 2.1 | 12.50 ± 0.32 | Overproduction, iodine++ |
| Parameter | Value | Source |
|---|---|---|
| Optimal pH | 6.5–7.5 | |
| Substrate specificity | 3–4 glucose branch chains | |
| KM (maltotetraose) | 0.15 mM |
Recombinant GlgX has potential applications in:
Glycogen engineering: Modifying chain-length distributions for industrial polysaccharides.
Metabolic studies: Elucidating glycogen turnover in biofilms and stress responses .
KEGG: ecx:EcHS_A3631