EC Number   |
General Information |
Reference |
|---|
   5.1.3.20 | malfunction |
a HP0859 knockout mutant shows a severe loss of lipopolysaccharide structure and a significant reduction of adhesion levels in an infection model to human stomach gastric adenocarcinoma AGS cells, if compared with the wild-type strain |
-, 727070 |
| 5.1.3.20 | malfunction |
the Escherichia coli rfaD-deletion mutant strain WJW00 can synthesize Kdo2-lipid A. 3-Deoxy-D-manno-oct-2-ulosonic acid (Kdo)2-lipid A is the conserved structure domain of lipopolysaccharide found in most Gram-negative bacteria, and is believed to stimulate the human innate immune system through the TLR4/MD2 complex. Kdo2-lipid A is an important stimulator for studying the mechanism of the innate immune system and for developing bacterial vaccine adjuvants. Compared with the wild-type strain W3110, WJW00 shows increased hydrophobicity, higher cell permeability, greater autoaggregation and decreased biofilm-forming ability. Phenotypes, overview |
-, 748527 |
| 5.1.3.20 | metabolism |
last enzyme in the pathway that produces L-glycero-D-manno-heptose starting from sedoheptulose-7-phosphate |
-, 727070 |
| 5.1.3.20 | more |
an N-terminal seven-stranded modified Rossmann fold where the NAD+ cofactor is bound and a smaller C-terminal alpha/beta domain are responsible for the binding of the substrate |
-, 727070 |
| 5.1.3.20 | more |
the enzyme contains a catalytic triad involved in catalyzing hydride transfer with the aid of NADP+. The enzyme may recognize their substrate in a lock-and-key fashion, binding analysis, docking study, enzyme structure comparisons, detailed overview |
-, 726590 |
