Literature summary for 4.2.1.30 extracted from
Jiang, W.; Wang, S.; Yang, Z.; Fang, B.
B12-independent glycerol dehydratase and its reactivase from Clostridia butyricum Optimizing cloning by uniform design logic (2015), Eng. Life Sci., 15, 519-524 .
No PubMed abstract available
Application
Application |
Comment |
Organism |
synthesis |
enzymatic production of 1,3-propanediol, which is a compound of great potential application in many synthesis reactions, in particular as a monomer for polycondensations to produce polyethers, polyurethanes, and polyesters. An optimal PCR system is developed for effective and reproducible PCR amplification of unknown long gene segments from the genome. Using this method, a new glycerol dehydratase is obtained, which eliminates the need for coenzyme B12. This reduces the cost of 1,3-propanediol production from renewable resources |
Clostridium butyricum |
Cloned(Commentary)
Cloned (Comment) |
Organism |
cloning of B12-independent glycerol dehydratase and its reactivase from Clostridium butyricum VPI1718, and expression in Escherichia coli BL21 (DE3). The activity of glycerol dehydratase activity is six times higher than in Clostridium butyricum |
Clostridium butyricum |
Organism
Organism |
UniProt |
Comment |
Textmining |
Clostridium butyricum |
Q8GEZ8 AND Q8GEZ7 |
Q8GEZ8: gene dhaB1, Q8GEZ7: gene dhaB2 |
- |
Clostridium butyricum VPI 1718 |
Q8GEZ8 AND Q8GEZ7 |
Q8GEZ8: gene dhaB1, Q8GEZ7: gene dhaB2 |
- |
Synonyms
Synonyms |
Comment |
Organism |
B12-independent glycerol dehydratase |
- |
Clostridium butyricum |
GDHt |
- |
Clostridium butyricum |
Cofactor
Cofactor |
Comment |
Organism |
Structure |
additional information |
cloning of B12-independent glycerol dehydratase |
Clostridium butyricum |
|