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
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4.3.1.19
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valine
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pyridoxal
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l-isoleucine
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4.2.1.16
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alpha-ketobutyrate
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2-ketobutyrate
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l-serine
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homoserine
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isoleucine-valine
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acetohydroxy
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acetolactate
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citramalate
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attenuata
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feedback-resistant
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2-oxobutyrate
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acetohydroxyacid
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sinoatrial
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molecular biology
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synthesis
- 4.3.1.19
- valine
- pyridoxal
- l-isoleucine
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4.2.1.16
- alpha-ketobutyrate
- 2-ketobutyrate
- l-serine
- homoserine
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isoleucine-valine
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acetohydroxy
- acetolactate
- citramalate
- attenuata
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feedback-resistant
- 2-oxobutyrate
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acetohydroxyacid
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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
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Engineering
Engineering on EC 4.3.1.19 - threonine ammonia-lyase
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E520A
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omr1-7 allele, tolerates high concentrations of L-O-methylthreonine
H542L
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omr1-8 allele, tolerates high concentrations of L-O-methylthreonine
R499C
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omr1-5 allele, tolerates high concentrations of L-O-methylthreonine
R499C/R544H
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omr1-1 allele, tolerates high concentrations of L-O-methylthreonine
Y449L
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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
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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
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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
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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
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site-directed mutagenesis, the mutant acts similar to the wild-type
Q347A
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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
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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
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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
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feedback inhibition by L-Ile is entirely abolished, so that the enzyme is always present in a relaxed high-activity state
F383A
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the mutant enzyme shows complete resistance to feedback inhibition by isoleucine
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V140M
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the specific activity of V140M mutant enzyme is 1.5fold higher than that of the wild-type enzyme
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V140M/F383A
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the mutant enzyme displays 1.5fold specific activity and complete resistance to isoleucine
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A14T
the mutant enzyme shows higher thermostability than wild-type enzyme without considerable loss in activity
E347F
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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the enzyme from the regulatory mutant CU18 is indistinguishable from the wild type enzyme in molecular weight and subunit composition
additional information
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mutants lacking yjgF generate an isoleucine-insensitive protein
additional information
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mutant with an activator site-deficient enzyme form, the Km for L-Thr is increased 4fold as compared with the wild type enzyme