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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Inhibitors
Inhibitors on EC 4.3.1.19 - threonine ammonia-lyase
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L-Cycloserine
powerful suicide inactivator that generates a covalent pyridoxal 5'-phosphate-isoxazole complex
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20 mM, about 50% inhibition. Inhibition is not reversed by AMP
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20 mM, about 50% inhibition. Inhibition is not reversed by AMP
Ile
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2 enzyme forms: an isoleucine-sensitive enzyme form and and isoleucine-insensitive form, pH-dependence of inhibition
Ile
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native enzyme is totally inhibited by 15 mM Ile, the heterologous catabolic enzyme from E. coli retains 60% of its original activity even in presence of 200 mM Ile
Ile
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competitive allosteric inhibitor, the enzyme exists in two distinct catalytically active species: a tetramer sensitive to L-Ile inhibition and a dimer insensitive to L-Ile inhibition
Ile
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0.5 mM, wild type enzyme is completely inhibited at both pH 8.0 and pH 6.5, the mutant enzyme is sensitive only at pH 6.5. In contrast to the wild type enzyme 1 mM Val does not reverse L-Ile inhibition of the mutant enzyme
Ile
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2 different forms: one enzyme form is sensitive to inhibition by Ile, the other form is insensitive to inhibition by Ile
Ile
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feed-back inhibition; HgCl2 treated enzyme is less sensitive; L-Val partially reverses inhibition
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activation below 0.01 mM, strong inhibition above, 50% inhibition at 0.064 mM, inhibition can be reversed by valine
isoleucine
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allosteric effector inducing dimerization, inhibition is reversed by high concentrations of valine
isoleucine
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end product inhibition, reversed by valine, the short C-terminal regulatory domain is composed of one ACT-like subdomain, which binds isoleucine and valine
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at 1 mM the transgenic lines containing omr1-1, omr1-5, and omr1-8 have 85% activity, while the transgenic line containing omr1-7 has 70% activity, the wild-type has 20% activity
L-isoleucine
less than 2% activity remains after addition of 0.5 mM L-isoleucine
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20 mM, about 50% inhibition. Inhibition is not reversed by AMP
pyruvate
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uncompetitive inhibition and substrate inhibition with respect to L-Thr, noncompetitive inhibition with respect to AMP
pyruvate
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noncompetitive inhibition with respect to L-Thr, mixed type inhibition with respect to AMP
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feedback-inhibition of threonine deaminase by branched-chain amino acids
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additional information
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feedback-inhibition of threonine deaminase by branched-chain amino acids
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additional information
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feedback-inhibition of threonine deaminase by branched-chain amino acids
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