4.3.1.19: threonine ammonia-lyase
This is an abbreviated version!
For detailed information about threonine ammonia-lyase, go to the full flat file.
Word Map on EC 4.3.1.19
-
4.3.1.19
-
valine
-
pyridoxal
-
l-isoleucine
-
4.2.1.16
-
alpha-ketobutyrate
-
2-ketobutyrate
-
l-serine
-
homoserine
-
isoleucine-valine
-
acetohydroxy
-
acetolactate
-
citramalate
-
attenuata
-
feedback-resistant
-
2-oxobutyrate
-
acetohydroxyacid
-
sinoatrial
-
molecular biology
-
synthesis
- 4.3.1.19
- valine
- pyridoxal
- l-isoleucine
-
4.2.1.16
- alpha-ketobutyrate
- 2-ketobutyrate
- l-serine
- homoserine
-
isoleucine-valine
-
acetohydroxy
- acetolactate
- citramalate
- attenuata
-
feedback-resistant
- 2-oxobutyrate
-
acetohydroxyacid
-
sinoatrial
- molecular biology
- synthesis
Reaction
Synonyms
BsBTD1, CgBTD1, CgCTD, EC 4.2.1.16, EcBTD2, EcCTD, FgIlv1, GSU0486, ilvA, L-TD, L-TDH, L-threonine deaminase, L-threonine dehydratase, MSMEG3183, OMR1, PpBTD2, pTD2, SaBTD1, SaCTD, SgBTD1, SlTD1, SlTD2, sp0454, TD, TD1, TD2, tdcB, TDH, TH, Thr ammonia-lyase, threonine ammonia-lyase, Threonine deaminase, threonine deaminase/dehydratase, threonine dehydrase, threonine dehydratase, threonine dehydratase/deaminase
ECTree
Advanced search results
Application
Application on EC 4.3.1.19 - threonine ammonia-lyase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
molecular biology
-
in contrast to the wild-type, all four transgenic TD lines are able to tolerate high concentrations of L-O-methylthreonine. This illustrates the potential use of these mutant omr genes as dominant selectable markers in plant transformation
synthesis
-
production of poly(3-hydroxybutyrate-co-3-hydroxyvalerate) from a single unrelated carbon source via threonine biosynthesis in Escherichia coli, by overexpression of threonine deaminase, which is the key factor for providing propionyl-coenzyme A (propionyl-CoA), from different host bacteria, removal of the feedback inhibition of threonine by mutating and overexpressing the thrABC operon in Escherichia coli, and knock-out of the competitive pathways of catalytic conversion of propionyl-CoA to 3-hydroxyvaleryl-CoA. Construction of a series of strains and mutants leads to production of the poly(3-hydroxybutyrate-co-3-hydroxyvalerate) copolymer with differing monomer compositions in a modified M9 medium supplemented with 20 g/liter xylose. The largest 3-hydroxyvalerate fraction obtained in the copolymer is 17.5 mol%
synthesis
the mutant L-threonine deaminase G323D/F510L/T344A together with thermostable L-leucine dehydrogenase from Bacillus sphaericus DSM730 and formate dehydrogenase from Candida boidinii constitute a one-pot system for biosynthesis of L-2-aminobutyric acid