Cloned (Comment) | Organism |
---|---|
recombinant enzyme expression in Escherichia coli, coexpression with N-acetylneuraminic acid lyase from Corynebacterium glutamicum ATCC 13032 (CgNal, EC 4.1.3.3) | Anabaena sp. CH1 |
Protein Variants | Comment | Organism |
---|---|---|
additional information | metabolic channeling enables efficient transfer of the intermediates by forming a multienzyme complex. To leverage the metabolic channeling for improved biosynthesis, N-acetylneuraminic acid lyase from Corynebacterium glutamicum ATCC 13032 (CgNal, EC 4.1.3.3) and N-acetylglucosamine-2-epimerase from Anabaena sp. CH1 (anAGE) are coexpressed in Escherichia coli and the whole cell are used to synthesize N-acetylneuraminic acid (Neu5Ac) from N-acetylglucosamine (GlcNAc) and pyruvate. To get the multienzyme complex, a polycistronic plasmid with high levels of CgNal and anAGE expression is constructed by tuning the orders of the genes. The Shine-Dalgarno (SD) sequence and aligned spacing (AS) distance are optimized. The Escherichia coli strain Rosetta harboring the polycistronic plasmid pET-28a-SD2-AS1-CgNal-SD-AS-anAGE increases the production of Neu5Ac by 58.7% to 92.5 g/l in 36 h by whole-cell catalysis and by 21.9% up to 112.8 g/l in 24 h with the addition of Triton X-100 | Anabaena sp. CH1 |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
N-Acyl-D-glucosamine | Anabaena sp. CH1 | - |
N-Acyl-D-mannosamine | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Anabaena sp. CH1 | A4UA16 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
N-Acyl-D-glucosamine | - |
Anabaena sp. CH1 | N-Acyl-D-mannosamine | - |
r |
Synonyms | Comment | Organism |
---|---|---|
AGE | - |
Anabaena sp. CH1 |
anAGE | - |
Anabaena sp. CH1 |