Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.6.99.2 extracted from

  • Commichau, F.M.; Alzinger, A.; Sande, R.; Bretzel, W.; Reuss, D.R.; Dormeyer, M.; Chevreux, B.; Schuldes, J.; Daniel, R.; Akeroyd, M.; Wyss, M.; Hohmann, H.P.; Pragai, Z.
    Engineering Bacillus subtilis for the conversion of the antimetabolite 4-hydroxy-l-threonine to pyridoxine (2015), Metab. Eng., 29, 196-207.
    View publication on PubMed
Search for more literature for 2.6.99.2

Protein Variants

Protein Variants Comment Organism
synthesis engineering of a Bacillus subtilis strain that forms significant amounts of pyridoxine via a non-native deoxyxylulose 5'-phosphate-(DXP)-dependent vitamin B6 pathway. The pathway consists of the 4-hydroxy-L-threonine-phosphate dehydrogenase PdxA, the pyridoxine 5'-phosphate synthase PdxJ and the native DXP synthase, Dxs. Bacteria are adapted to tolerate the antimetabolite 4-HO-Thro in order to allow feeding of high amounts of 4-hydroxy-threonine (4-HO-Thr) that can be converted to pyridoxine. The adapted bacteria produce 28–34 mg/l pyridoxine from 4-HO-Thr while the wild-type parent produced 12 mg/l pyridoxine. Identification of a better combination of pdxA and pdxJ alleles results in production of 65 mg/l pyridoxine Sinorhizobium meliloti

Organism

Organism UniProt Comment Textmining
Sinorhizobium meliloti
-
-
-
Sinorhizobium meliloti IFO14782
-
-
-

Synonyms

Synonyms Comment Organism
PdxJ
-
 Sinorhizobium meliloti