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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

Reaction

2-aminobut-2-enoate
=
2-iminobutanoate

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

     4 Lyases
         4.3 Carbon-nitrogen lyases
             4.3.1 Ammonia-lyases
                4.3.1.19 threonine ammonia-lyase

Engineering

Engineering on EC 4.3.1.19 - threonine ammonia-lyase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E520A
-
omr1-7 allele, tolerates high concentrations of L-O-methylthreonine
H542L
-
omr1-8 allele, tolerates high concentrations of L-O-methylthreonine
R499C
-
omr1-5 allele, tolerates high concentrations of L-O-methylthreonine
R499C/R544H
-
omr1-1 allele, tolerates high concentrations of L-O-methylthreonine
Y449L
-
concentration of isoleucine needed to reach 50% inhibition increases by a factor 45, two different effector-binding sites are constituted in part by Y449 and Y543
Y543L
-
concentration of isoleucine needed to reach 50% inhibition increases by a factor 38, two different effector-binding sites are constituted in part by Y449 and Y543
G350A
-
site-directed mutagenesis, the affinity for both allosteric effectors is lower compared to the wild-type, valine binds exclusively to the R state, the mutation causes a shift in the equilibrium between the T and R conformational states of the protein toward the T state with L being higher than that of the wild-type enzyme
L352A
-
site-directed mutagenesis, the affinity for both allosteric effectors is lower compared to the wild-type, valine binds exclusively to the R state, the mutation causes a shift in the equilibrium between the T and R conformational states of the protein toward the T state with L being 6.5fold higher than that of the wild-type enzyme
N363A
-
site-directed mutagenesis, the mutant acts similar to the wild-type
Q347A
-
site-directed mutagenesis, mutant Q347A is very similar to the wild-type enzyme in most of its characteristics, except for a 1.5fold increase in L and a 5fold increase in KTIle
T367A
-
site-directed mutagenesis, the T367A mutation causes a decrease in the affinity of bsTD for both allosteric effectors and an increase in substrate affinity compared to the wild-type enzyme
Y371L
-
site-directed mutagenesis, the apparent affinities for both of the allosteric effectors are very low and the apparent dissociation constant for isoleucine from the T state is 50fold higher compared to the wild-type
F383A
the mutant enzyme shows complete resistance to feedback inhibition by isoleucine
V140M
the specific activity of V140M mutant enzyme is 1.5fold higher than that of the wild-type enzyme
V140M/F383A
the mutant enzyme displays 1.5fold specific activity and complete resistance to isoleucine
Val323Ala
-
feedback inhibition by L-Ile is entirely abolished, so that the enzyme is always present in a relaxed high-activity state
F383A
-
the mutant enzyme shows complete resistance to feedback inhibition by isoleucine
-
V140M
-
the specific activity of V140M mutant enzyme is 1.5fold higher than that of the wild-type enzyme
-
V140M/F383A
-
the mutant enzyme displays 1.5fold specific activity and complete resistance to isoleucine
-
A14T
the mutant enzyme shows higher thermostability than wild-type enzyme without considerable loss in activity
E347F
-
mutation decreases the K0.5 values of Thr without significant change of the n(H) value compared to wild-type. Mutant is strongly feedback-resistant to Ile compared to the wild-type enzyme. IC50 (Ile) is increased compared to wild-type
E442A
-
mutation increases the K0.5 value of Thr and n(H) value, comparing to those of the wild-type enzyme. IC50 (Ile) is decreased compared to wild-type
F352A
-
mutation decreases the K0.5 values of Thr without significant change of the n(H) value compared to wild-type. Mutant is strongly feedback-resistant to Ile compared to the wild-type enzyme. IC50 (Ile) is increased compared to wild-type
F352A/I460F
-
double mutant is more resistant to Ile inhibition than any single site mutant. Double mutations retains more than 85% activity even at 10 mM Ile
F352A/R362F
-
mutant shows both higher activity and stronger resistance to Ile inhibition compared to wild-type mice. Overexpression of mutant in Escherichia coli JW3591 significantly increases the production of ketobutyrate and Ile in comparison to the reference strains overexpressing wild-type
F510L
mutant enzyme with greater thermostability compared to wild-type enzyme
G323D
mutant enzyme with greater thermostability compared to wild-type enzyme
G323D/F510L/T344A
the half-life of mutant enzyme at 42°C increases from 10 to 210 min, a 20fold increase compared to the wild-type enzyme, and the temperature at which the activity of the enzyme decreases by 50% in 15 min increases from 39 to 53°C
G350E
-
mutation increases the K0.5 value of Thr and n(H) value, comparing to those of the wild-type enzyme. IC50 (Ile) is decreased compared to wild-type
G445E
-
mutation G445E increased the K0.5 value of Thr without change of n(H) value compared to wild-type. IC50 (Ile) is slightly increased compared to wild-type
I460F
-
mutation decreases the K0.5 values of Thr without significant change of the n(H) value compared to wild-type. Mutant is strongly feedback-resistant to Ile compared to the wild-type enzyme. IC50 (Ile) is increased compared to wild-type
I460F/R362F
-
double mutant is more resistant to Ile inhibition than any single site mutant. Double mutations retains more than 85% activity even at 10 mM Ile
R362F
-
mutation decreases the K0.5 values of Thr without significant change of the n(H) value compared to wild-type. Mutant is strongly feedback-resistant to Ile compared to the wild-type enzyme. IC50 (Ile) is increased compared to wild-type
R449C
the mutant enzyme shows higher thermostability than wild-type enzyme without considerable loss in activity
T344A
the mutant enzyme shows higher thermostability than wild-type enzyme without considerable loss in activity
Y369L
-
mutant shows an 91fold increased IC50 (Ile) value compared to wild-type
K67A
inactive mutant enzyme, the mutant enzyme is not yellow, as observed for the wild-type enzyme
K67Q
inactive mutant enzyme, the mutant enzyme is not yellow, as observed for the wild-type enzyme
additional information