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Information on EC 4.3.1.19 - threonine ammonia-lyase and Organism(s) Solanum lycopersicum and UniProt Accession P25306

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EC Tree
     4 Lyases
         4.3 Carbon-nitrogen lyases
             4.3.1 Ammonia-lyases
                4.3.1.19 threonine ammonia-lyase
IUBMB Comments
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 . The enzymes from a number of sources also act on L-serine, cf. EC 4.3.1.17, L-serine ammonia-lyase.
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This record set is specific for:
Solanum lycopersicum
UNIPROT: P25306
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Word Map
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The taxonomic range for the selected organisms is: Solanum lycopersicum
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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L-threonine
=
2-oxobutanoate
+
NH3
=
+
Synonyms
threonine deaminase, threonine dehydratase, sactd, threonine ammonia-lyase, sp0454, fgilv1, l-tdh, threonine dehydratase/deaminase, threonine dehydrase, threonine deaminase/dehydratase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pTD2
processed form of TD2, the C-terminal regulatory domain is removed
SlTD1
isoform, involved in isoleucine biosynthesis in plants
SlTD2
isoform, for plant defense the protein is involved in threonine degradation in leaf eating insects
Threonine deaminase
-
L-TDH
-
-
-
-
L-threonine deaminase
-
-
-
-
L-threonine dehydratase
-
-
-
-
TD
-
-
-
-
TDH
-
-
-
-
Threonine deaminase
-
-
-
-
threonine deaminase/dehydratase
-
-
threonine dehydrase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Deamination
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9024-34-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-Ser
pyruvate + NH3
show the reaction diagram
-
-
-
-
?
L-Thr
?
show the reaction diagram
-
key enzyme in biosynthesis of Ile
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-Thr
?
show the reaction diagram
-
key enzyme in biosynthesis of Ile
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ile
-
2 different forms: one enzyme form is sensitive to inhibition by Ile, the other form is insensitive to inhibition by Ile
additional information
-
feedback-inhibition of threonine deaminase by branched-chain amino acids
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3
L-serine
processed TD2
2.3
L-threonine
processed TD2
0.25 - 1.7
L-Ser
0.25
L-Thr
-
Ile-sensitive enzyme form and Ile-insensitive form
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
the enzyme is highly active in an alkaline pH range, little or no activity is observed at pH values below 6.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
active over a wide range of temperatures, optimal enzyme activity is observed at 58°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
isoleucine-sensitive enzyme form occurs predominantly in younger leaves, isoleucine-insensitive enzyme form occurs predominantly in older leaves
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
involved in methionine metabolism, plays a predominant role in isoleucine synthesis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TD2_SOLLC
595
0
64937
Swiss-Prot
Chloroplast (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
molecular mass of processed TD2 determined by SDS-PAGE
55000
determined by Western blot analysis, mature TD2
66180
predicted molecular mass of SlTD1
200000
-
Ile-insensitive enzyme form, gel filtration
370000
-
Ile-sensitive enzyme form, gel filtration
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
using a Sephadex G-25, a DEAE-cellulose DE52, a HiLoad26/60 Superdex 200 and a HiPrep 16/10 column
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a modified SlTD2 cDNA is cloned into the pET30a+ vector producing a truncated form of SlTD2 lacking the 51 amino acids corresponding to the N-terminal chloroplast-targeting sequence
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
about 500 times higher transcript levels in flowers than in leaves or roots
-
induced transcription in response to osmotic stress
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Szamosi, I.; Shaner, D.L.; Singh, B.K.
Identification and characterization of a biodegradative form of threonine dehydratase in senescing tomato (Lycopersicon esculentum) leaf
Plant Physiol.
101
999-1004
1993
Solanum lycopersicum
Manually annotated by BRENDA team
Chen, H.; Gonzales-Vigil, E.; Wilkerson, C.G.; Howe, G.A.
Stability of plant defense proteins in the gut of insect herbivores
Plant Physiol.
143
1954-1967
2007
Solanum lycopersicum (P25306)
Manually annotated by BRENDA team
Joshi, V.; Joung, J.G.; Fei, Z.; Jander, G.
Interdependence of threonine, methionine and isoleucine metabolism in plants: accumulation and transcriptional regulation under abiotic stress
Amino Acids
39
933-947
2010
Arabidopsis thaliana, Solanum lycopersicum, Nicotiana sp.
Manually annotated by BRENDA team