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
-
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
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Systematic Name
Systematic Name on EC 4.3.1.19 - threonine ammonia-lyase
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L-threonine ammonia-lyase (2-oxobutanoate-forming)
Most enzymes that catalyse this reaction are pyridoxal-phosphate-dependent, although some enzymes contain an iron-sulfur cluster instead. The reaction catalysed by both types of enzymes involves the initial elimination of water to form an enamine intermediate (hence the enzyme's original classification as EC 4.2.1.16, threonine dehydratase), followed by tautomerization to an imine form and hydrolysis of the C-N bond [3,5]. The latter reaction, which can occur spontaneously, is also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase [5]. The enzymes from a number of sources also act on L-serine, cf. EC 4.3.1.17, L-serine ammonia-lyase.