Information on EC 4.3.1.19 - threonine ammonia-lyase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY
4.3.1.19
-
RECOMMENDED NAME
GeneOntology No.
threonine ammonia-lyase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2-aminobut-2-enoate = 2-iminobutanoate
show the reaction diagram
(1b), spontaneous
-
-
-
2-iminobutanoate + H2O = 2-oxobutanoate + ammonia
show the reaction diagram
(1c), spontaneous
-
-
-
L-threonine = 2-aminobut-2-enoate + H2O
show the reaction diagram
(1a)
-
-
-
L-threonine = 2-oxobutanoate + ammonia
show the reaction diagram
(overall reaction); that from P. putida is not. The enzyme from a number of sources also acts on L-serine, cf. EC 4.3.1.17, L-serine ammonia-lyase. The reaction catalysed probably involves initial elimination of water, hence the enzyme's original classification as EC 4.2.1.16, threonine dehydratase, followed by isomerization and hydrolysis of the product with C-N bond breakage; The enzyme from many sources is a pyridoxal-phosphate protein
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Deamination
-
-
-
-
elimination
-
-
elimination
Q9AXU4
-
elimination
P25306
-
elimination
-
-
alpha,beta-position of amino acid; beta-position of amino acid; of NH3, alpha,beta-position of amino acid
-
PATHWAY
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
Glycine, serine and threonine metabolism
-
Metabolic pathways
-
Valine, leucine and isoleucine biosynthesis
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
EC 4.2.1.16
-
-
formerly
-
EC 4.2.1.16
-
formerly
GSU0486
Q74FW6
-
GSU0486
Geobacter sulfurreducens DL-1
Q74FW6
-
-
L-TDH
-
-
-
-
L-threonine deaminase
-
-
-
-
L-threonine dehydratase
-
-
-
-
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
TD
-
-
-
-
tdcB
Geobacter sulfurreducens DL-1
Q74FW6
-
-
TDH
-
-
-
-
Thr ammonia-lyase
Q74FW6
-
Thr ammonia-lyase
Geobacter sulfurreducens DL-1
Q74FW6
-
-
threonine ammonia-lyase
Q74FW6
-
threonine ammonia-lyase
Geobacter sulfurreducens DL-1
Q74FW6
-
-
Threonine deaminase
-
-
-
-
Threonine deaminase
-
-
Threonine deaminase
-
-
Threonine deaminase
-
-
Threonine deaminase
Q9AXU4
-
Threonine deaminase
-
-
Threonine deaminase
-
-
-
Threonine deaminase
-
-
Threonine deaminase
-
-
threonine deaminase/dehydratase
-
-
threonine dehydrase
-
-
-
-
threonine dehydratase
-
-
threonine dehydratase/deaminase
-
-
CAS REGISTRY NUMBER
COMMENTARY
9024-34-4
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Anacystis marina
-
-
-
Manually annotated by BRENDA team
2 enzyme forms: an isoleucine-sensitive enzyme form and and an isoleucine-insensitive form
-
-
Manually annotated by BRENDA team
2 enzyme forms: an isoleucine-sensitive enzyme form and and an isoleucine-insensitive form; strain Ok-79-fl
-
-
Manually annotated by BRENDA team
Chloroflexus aurantiacus Ok-79-fl
strain Ok-79-fl
-
-
Manually annotated by BRENDA team
strain F5, N.C.I.B. 11102
-
-
Manually annotated by BRENDA team
Corynebacterium sp. F5
strain F5, N.C.I.B. 11102
-
-
Manually annotated by BRENDA team
Japanese quail, male
-
-
Manually annotated by BRENDA team
Cyclotella nana
-
-
-
Manually annotated by BRENDA team
a genetically derepressed mutant strain of Escherichia coli K12; biosynthetic threonine deaminase; the enzyme exists in two distinct catalytically active species: a tetramer sensitive to L-Ile inhibition and a dimer insensitive to L-Ile inhibition
-
-
Manually annotated by BRENDA team
ATCC 14948; biodegradative threonine dehydratase; strain K 12
-
-
Manually annotated by BRENDA team
biodegradative threonine dehydratase
-
-
Manually annotated by BRENDA team
biosynthetic threonine deaminase
-
-
Manually annotated by BRENDA team
biosynthetic threonine deaminase; strain K 12
-
-
Manually annotated by BRENDA team
ilvA mutant encoding an enzyme that is resistant to feedback inhibition by L-Ile
-
-
Manually annotated by BRENDA team
regulatory mutant CU18
-
-
Manually annotated by BRENDA team
strain K 12
-
-
Manually annotated by BRENDA team
Escherichia coli K 12
strain K 12
-
-
Manually annotated by BRENDA team
strain SM-ZK, dehydratase I and dehydratase II
-
-
Manually annotated by BRENDA team
Euglena gracilis SM-ZK
strain SM-ZK, dehydratase I and dehydratase II
-
-
Manually annotated by BRENDA team
strain DL-1, ATCC 51573, gene GSU0486 or tcdB
UniProt
Manually annotated by BRENDA team
Geobacter sulfurreducens DL-1
strain DL-1, ATCC 51573, gene GSU0486 or tcdB
UniProt
Manually annotated by BRENDA team
Hansenula henricii
-
-
-
Manually annotated by BRENDA team
strain AKU 0084,biosynthetic threonine deaminase
-
-
Manually annotated by BRENDA team
Morganella morganii AKU 0084
strain AKU 0084,biosynthetic threonine deaminase
-
-
Manually annotated by BRENDA team
strain PAC1
-
-
Manually annotated by BRENDA team
Pseudomonas aeruginosa PAC1
strain PAC1
-
-
Manually annotated by BRENDA team
strain Lz4W, gene ilvA
-
-
Manually annotated by BRENDA team
strain Lz4W, gene ilvA
-
-
Manually annotated by BRENDA team
biosynthetic threonine deaminase
-
-
Manually annotated by BRENDA team
biodegradative threonine dehydratase
-
-
Manually annotated by BRENDA team
biodegradative threonine dehydratase; strain LT2
-
-
Manually annotated by BRENDA team
mutant with an activator site-deficient enzyme form
-
-
Manually annotated by BRENDA team
ATCC 25419
-
-
Manually annotated by BRENDA team
strain IHr313, strain 149 lacks L-threonine dehydratase
-
-
Manually annotated by BRENDA team
2 different forms: one enzyme form is sensitive to inhibition by Ile, the other form is insensitive to inhibition by Ile
-
-
Manually annotated by BRENDA team
i.e. Agmenellum quadruplicatum
-
-
Manually annotated by BRENDA team
Tetraselmis maculata
-
-
-
Manually annotated by BRENDA team
Thermus sp. X-1
X-1
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
reduced threoinine deaminase causes severe growth defects
metabolism
-
involved in methionine metabolism, plays a predominant role in isoleucine synthesis
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
beta-chloro-L-Ala
?
show the reaction diagram
-
-
-
-
?
beta-chloro-L-Ala
?
show the reaction diagram
Morganella morganii AKU 0084
-
-
-
-
?
DL-allo-cystathionine
?
show the reaction diagram
-
at 20% of the activity with L-Thr
-
-
-
L-allothreonine
?
show the reaction diagram
Corynebacterium sp., Corynebacterium sp. F5
-
5% of the activity L-Thr
-
-
?
L-Cys
?
show the reaction diagram
Morganella morganii, Morganella morganii AKU 0084
-
-
-
-
?
L-homoserine
2-oxobutanoate + NH3 + H2O
show the reaction diagram
-
-
-
-
?
L-Ser
pyruvate + NH3
show the reaction diagram
-
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
-
-
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
no activity
-
-
-
L-serine
pyruvate + NH3
show the reaction diagram
-
dehydratase I: 26% of the activity with L-Thr, dehydratase II: 16% of the activity with L-Thr
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
6% of the activity with L-Thr
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
20% of the activity with L-Ser
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
rapid loss of activity during Ser deamination
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
-
45% of the activity with L-Thr
-
-
-
L-serine
pyruvate + NH3
show the reaction diagram
-
isoleucine-insensitive enzyme
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
Thermus sp. X-1
-
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
Pseudomonas aeruginosa PAC1
-
20% of the activity with L-Ser
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
Corynebacterium sp. F5
-
6% of the activity with L-Thr
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
Morganella morganii AKU 0084
-
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
Chloroflexus aurantiacus Ok-79-fl
-
-
-
-
?
L-serine
pyruvate + NH3
show the reaction diagram
Euglena gracilis SM-ZK
-
dehydratase I: 26% of the activity with L-Thr, dehydratase II: 16% of the activity with L-Thr
-
-
?
L-Thr
?
show the reaction diagram
-
inducible enzyme
-
-
-
L-Thr
?
show the reaction diagram
-
constitutive enzyme
-
-
-
L-Thr
?
show the reaction diagram
-
constitutive enzyme
-
-
-
L-Thr
?
show the reaction diagram
-
first reaction of the Ile pathway
-
-
-
L-Thr
?
show the reaction diagram
-
key enzyme in biosynthesis of Ile
-
-
-
L-Thr
?
show the reaction diagram
-
the enzyme is an important element in the flux control of Ile biosynthesis
-
-
-
L-Thr
?
show the reaction diagram
-
isoleucine-insensitive enzyme is subject to glucose-mediated catabolite repression
-
-
-
L-Thr
?
show the reaction diagram
-
increase of activity under gluconeogenic conditions in adult-rat hepatocytes cultured on collagen gel/nylon mesh
-
-
-
L-Thr
?
show the reaction diagram
-
the enzyme is formed under anaerobic conditions, the enzyme is induced by L-Ser and L-Thr, cAMP is required for the synthesis of the enzyme
-
-
-
L-Thr
?
show the reaction diagram
Corynebacterium sp. F5
-
constitutive enzyme
-
-
-
L-Thr
?
show the reaction diagram
Chloroflexus aurantiacus Ok-79-fl
-
isoleucine-insensitive enzyme is subject to glucose-mediated catabolite repression
-
-
-
L-Thr
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
P25306
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
Synechococcus sp. PCC 7002, Anacystis marina, Chroomonas salina, Hemiselmis virescens, Tetraselmis maculata, Cyclotella nana
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
Q9AXU4
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-, Q74FW6
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-, Q74FW6
a step in the pathway for the biosynthesis of isoleucine via isoleucine precursor 2-oxobutanoate generated from threonine, this pathway accounts for a minor fraction of isoleucine biosynthesis, while the majority of isoleucine is instead derived from acetyl-coenzyme A and pyruvate, possibly via the citramalate pathway, overview
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
biodegradation of L-threonine, the enzyme is involved in the biosynthetis pathway for isoleucine production, which is competitng with the valine biosynthetic pathway for the second precursor pyruvate
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
threonine deaminase is a key regulatory enzyme in the pathway for the biosynthesis of isoleucine, allosteric enzyme regulation model, overview
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
Thermus sp. X-1
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
Pseudomonas aeruginosa PAC1
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-, biodegradation of L-threonine, the enzyme is involved in the biosynthetis pathway for isoleucine production, which is competitng with the valine biosynthetic pathway for the second precursor pyruvate
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
Geobacter sulfurreducens DL-1
Q74FW6
-, a step in the pathway for the biosynthesis of isoleucine via isoleucine precursor 2-oxobutanoate generated from threonine, this pathway accounts for a minor fraction of isoleucine biosynthesis, while the majority of isoleucine is instead derived from acetyl-coenzyme A and pyruvate, possibly via the citramalate pathway, overview
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
Escherichia coli K 12
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
Escherichia coli K 12
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
Escherichia coli K 12
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
Escherichia coli K 12
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
Corynebacterium sp. F5
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
Morganella morganii AKU 0084
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
Chloroflexus aurantiacus Ok-79-fl
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
Euglena gracilis SM-ZK
-
-
-
?
additional information
?
-
-
when pyridoxamine 5'-phosphate is incubated with the apoenzyme in the presence of small quantities of keto acids, e.g. pyruvate or 2-oxobutanoate, small amounts of L-Ala or L-aminobutanoate are formed, the reaction is not reversible
-
-
-
additional information
?
-
-, Q74FW6
GSU0486 also catalyzes the deamination of L-serine, EC 4.3.1.17
-
-
-
additional information
?
-
Geobacter sulfurreducens DL-1
Q74FW6
GSU0486 also catalyzes the deamination of L-serine, EC 4.3.1.17
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-serine
pyruvate + NH3
show the reaction diagram
-
-
-
?
L-Thr
?
show the reaction diagram
-
inducible enzyme
-
-
-
L-Thr
?
show the reaction diagram
-
constitutive enzyme
-
-
-
L-Thr
?
show the reaction diagram
-
constitutive enzyme
-
-
-
L-Thr
?
show the reaction diagram
-
first reaction of the Ile pathway
-
-
-
L-Thr
?
show the reaction diagram
-
key enzyme in biosynthesis of Ile
-
-
-
L-Thr
?
show the reaction diagram
-
the enzyme is an important element in the flux control of Ile biosynthesis
-
-
-
L-Thr
?
show the reaction diagram
-
isoleucine-insensitive enzyme is subject to glucose-mediated catabolite repression
-
-
-
L-Thr
?
show the reaction diagram
-
increase of activity under gluconeogenic conditions in adult-rat hepatocytes cultured on collagen gel/nylon mesh
-
-
-
L-Thr
?
show the reaction diagram
-
the enzyme is formed under anaerobic conditions, the enzyme is induced by L-Ser and L-Thr, cAMP is required for the synthesis of the enzyme
-
-
-
L-Thr
?
show the reaction diagram
Corynebacterium sp. F5
-
constitutive enzyme
-
-
-
L-Thr
?
show the reaction diagram
Chloroflexus aurantiacus Ok-79-fl
-
isoleucine-insensitive enzyme is subject to glucose-mediated catabolite repression
-
-
-
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
P25306
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
Q9AXU4
-
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-, Q74FW6
a step in the pathway for the biosynthesis of isoleucine via isoleucine precursor 2-oxobutanoate generated from threonine, this pathway accounts for a minor fraction of isoleucine biosynthesis, while the majority of isoleucine is instead derived from acetyl-coenzyme A and pyruvate, possibly via the citramalate pathway, overview
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
biodegradation of L-threonine, the enzyme is involved in the biosynthetis pathway for isoleucine production, which is competitng with the valine biosynthetic pathway for the second precursor pyruvate
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
threonine deaminase is a key regulatory enzyme in the pathway for the biosynthesis of isoleucine, allosteric enzyme regulation model, overview
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
biodegradation of L-threonine, the enzyme is involved in the biosynthetis pathway for isoleucine production, which is competitng with the valine biosynthetic pathway for the second precursor pyruvate
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
Geobacter sulfurreducens DL-1
Q74FW6
a step in the pathway for the biosynthesis of isoleucine via isoleucine precursor 2-oxobutanoate generated from threonine, this pathway accounts for a minor fraction of isoleucine biosynthesis, while the majority of isoleucine is instead derived from acetyl-coenzyme A and pyruvate, possibly via the citramalate pathway, overview
-
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
ADP
-
no stimulation by ADP
AMP
-
activates
pyridoxal 5'-phosphate
-
required
pyridoxal 5'-phosphate
-
cofactor
pyridoxal 5'-phosphate
-
cofactor; Km: 0.00028 mM
pyridoxal 5'-phosphate
-
cofactor; contains 2 mol of pyridoxal 5'-phosphate per mol of enzyme
pyridoxal 5'-phosphate
-
cofactor; contains 2 mol of pyridoxal 5'-phosphate per mol of enzyme; contains 4 mol of pyridoxal 5'-phosphate per mol of enzyme
pyridoxal 5'-phosphate
-
required
pyridoxal 5'-phosphate
-
cofactor; tightly bound
pyridoxal 5'-phosphate
-
contains 4 mol of pyridoxal 5'-phosphate per mol of enzyme
pyridoxal 5'-phosphate
-
cofactor; contains 4 mol of pyridoxal 5'-phosphate per mol of enzyme
pyridoxal 5'-phosphate
-
contains 2 mol of pyridoxal 5'-phosphate per mol of enzyme
pyridoxal 5'-phosphate
-
cofactor
pyridoxal 5'-phosphate
-
required
pyridoxal 5'-phosphate
-
Km: 0.000682 mM; reactivates after dissociation of the coenzyme
pyridoxal 5'-phosphate
-
activates; reactivates after dissociation of the coenzyme
pyridoxal 5'-phosphate
-
cofactor; enzyme contains 1 mol of pyridoxal 5'-phosphate per 56000 Da subunit
pyridoxal 5'-phosphate
-
required
pyridoxal 5'-phosphate
-
1 mol per monomer
pyridoxal 5'-phosphate
-
1 molecule per monomer
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxamine 5'-phosphate
-
reactivates after dissociation of the coenzyme
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
K+
-
stimulates
K+
-
stimulates
K+
-
high requirement
K+
-
3fold increase in activity, half-maximal activation at 3.1 mM
Li+
-
stimulates
Na+
-
1.7fold increase in activity
NH4+
-
stimulates
NH4+
-
stimulates
Rb+
-
can partially replace K+ in activation
Li+
-
2.8fold increase in activity
additional information
-
no requirement for divalent cations
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2,2'-dithiodipyridine
Anacystis marina, Chroomonas salina, Cyclotella nana, Hemiselmis virescens, Porphyridium purpureum, Synechococcus sp. PCC 7002, Tetraselmis maculata
-
-
2-oxobutanoate
-
-
2-oxobutanoate
-
20 mM, about 50% inhibition. Inhibition is not reversed by AMP
2-oxoglutarate
-
-
Cys
-
L-Cys and D-Cys
formaldehyde
-
-
glyoxylate
-
20 mM, about 50% inhibition. Inhibition is not reversed by AMP
hydrazine
Anacystis marina, Chroomonas salina, Cyclotella nana, Hemiselmis virescens, Porphyridium purpureum, Synechococcus sp. PCC 7002, Tetraselmis maculata
-
-
hydroxylamine
-
-
hydroxylamine
-
-
hydroxylamine
Anacystis marina, Chroomonas salina
-
-
hydroxylamine
Cyclotella nana
-
reversed by pyridoxal 5'-phosphate
Ile
-
2 enzyme forms: an isoleucine-sensitive enzyme form and and isoleucine-insensitive form, pH-dependence of inhibition
Ile
-
50% inhibition at 0.14 mM Ile, 98% inhibition at 1 mM Ile
Ile
-
dehydratase I, 50% inhibition at 0.35 mM
Ile
-
Hg2+ protects
Ile
-
reversed by low concentrations of L-Val
Ile
-
feed-back inhibition; HgCl2 treated enzyme is less sensitive; L-Val partially reverses inhibition
Ile
-
0.06 mM, 50% inhibition
Ile
-
more sensitive at 40 C than at 65 C
Ile
-
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
-
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
-
feed-back inhibition
Ile
-
no inhibition
Ile
Cyclotella nana
-
-
Ile
-
2 different forms: one enzyme form is sensitive to inhibition by Ile, the other form is insensitive to inhibition by Ile
Ile
-
negative allosteric effector
Ile
-
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
-
biodegradative enzyme is feedback-resistant
Ile
-
reversed by Vla
iodoacetamide
Anacystis marina
-
-
iodoacetamide
Cyclotella nana
-
weak
iodoacetamide
Tetraselmis maculata
-
weak
iodoacetate
-
-
Isoleucine
-
activation below 0.01 mM, strong inhibition above, 50% inhibition at 0.064 mM, inhibition can be reversed by valine
Isoleucine
-
allosteric effector inducing dimerization, inhibition is reversed by high concentrations of valine
Isoleucine
-
feedback inhibition
Isoleucine
-
end product inhibition, reversed by valine, the short C-terminal regulatory domain is composed of one ACT-like subdomain, which binds isoleucine and valine
Isoniazid
Anacystis marina, Cyclotella nana, Porphyridium purpureum, Synechococcus sp. PCC 7002, Tetraselmis maculata
-
-
L-Cys
-
competitive
L-isoleucine
-
allosteric inhibition
L-isoleucine
-
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-Val
-
slight inhibition
Leu
-
dehydratase I, 6 mM, 50% inhibition
methoxylamine
Anacystis marina, Chroomonas salina, Cyclotella nana, Hemiselmis virescens, Porphyridium purpureum, Synechococcus sp. PCC 7002, Tetraselmis maculata
-
-
Na-chenodeoxycholate
-
-
Na-cholatemethyl ester
-
-
Na-deoxycholate
-
-
Na-lithocholate
-
-
NEM
Anacystis marina, Chroomonas salina, Cyclotella nana, Hemiselmis virescens, Porphyridium purpureum, Synechococcus sp. PCC 7002, Tetraselmis maculata
-
-
nitrate
-
-
-
NSD-1055
Anacystis marina, Chroomonas salina, Cyclotella nana, Hemiselmis virescens, Porphyridium purpureum, Synechococcus sp. PCC 7002, Tetraselmis maculata
-
-
p-Chloromercuriphenyl sulfonate
Anacystis marina, Chroomonas salina, Cyclotella nana, Hemiselmis virescens, Porphyridium purpureum, Synechococcus sp. PCC 7002, Tetraselmis maculata
-
-
phenylhydrazine
-
reversed by pyridoxal 5'-phosphate
phenylhydrazine
-
-
phenylhydrazine
Cyclotella nana
-
reversed by pyridoxal 5'-phosphate
phosphoenolpyruvate
-
-
pyruvate
-
uncompetitive inhibition and substrate inhibition with respect to L-Thr, noncompetitive inhibition with respect to AMP
pyruvate
-
noncompetitive inhibition with respect to L-Thr, mixed type inhibition with respect to AMP
pyruvate
-
20 mM, about 50% inhibition. Inhibition is not reversed by AMP
Semicarbazide
-
-
Semicarbazide
Anacystis marina, Cyclotella nana, Synechococcus sp. PCC 7002, Tetraselmis maculata
-
-
Ser
-
L-Ser, competitive with respect to L-Thr
additional information
Q74FW6
TcdB is not inhibited by isoleucine
-
additional information
-
feedback-inhibition of threonine deaminase by branched-chain amino acids
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Isoleucine
-
activation below 0.01 mM, strong inhibition above, 50% inhibition at 0.064 mM
L-Val
-
activates
L-Val
-
activates
L-Val
-
activates
NH4+
-
2.1fold increase in activity
phosphate
-
increases activity; maximal stimulation at 200 mM
additional information
-
dehydratase I and II: not affected by adenylates
-
additional information
-
no activation by AMP, ADP and ATP
-
additional information
-
threonine aldolase mutations increase substrate availability for threonine deaminase
-
additional information
Q9AXU4
the plant activates threonine deaminase in tissues attacked by herbivores
-
additional information
-
insensitive to the allosteric activation by AMP or CMP
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.25
-
L-Ser
-
Ile-insensitive enzyme form
1.7
-
L-Ser
-
Ile-sensitive form
5
-
L-Ser
-
in presence of AMP
8.9
-
L-Ser
-
in presence of AMP
10
-
L-Ser
-
Ile-insensitive enzyme
13.5
-
L-Ser
-
pH 9.0, 37C
30.3
-
L-Ser
-
in absence of AMP
40
-
L-Ser
-
in absence of AMP
61.8
-
L-Ser
-
-
3
-
L-serine
P25306
processed TD2
0.25
-
L-Thr
-
Ile-sensitive enzyme form and Ile-insensitive form
1.3
-
L-Thr
-
Ile-sensitive enzyme
1.5
-
L-Thr
-
in presence of 1 mM AMP
1.6
-
L-Thr
-
Ile-sensitive enzyme
2.5
-
L-Thr
-
in absence of phosphate
3
-
L-Thr
-
in presence of 50 mM phosphate
4
-
L-Thr
-
in presence of 250 mM phosphate
7.3
-
L-Thr
-
pH 9.0, 37C
11
-
L-Thr
-
in presence of AMP
13
-
L-Thr
-
dehydratase II
14
-
L-Thr
-
-
16
-
L-Thr
-
-
20
-
L-Thr
-
Ile-insensitive enzyme
21.3
-
L-Thr
-
Ile-sensitive enzyme
24
-
L-Thr
-
in absence of AMP
34
-
L-Thr
-
dehydratase I
70
-
L-Thr
-
without AMP
91
-
L-Thr
-
in absence of AMP
99.5
-
L-Thr
-
-
2.3
-
L-threonine
P25306
processed TD2
16
-
L-threonine
-
in the presence of 5 mM AMP
32
-
L-threonine
-
in the presence of 5 mM CMP
additional information
-
additional information
-
Monod-Wyman-Changeux symmetrical model analysis of steady-state kinetics for the wild-type and four mutant enzymes
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3
-
L-Ser
-
pH 9.0, 37C
5.2
-
L-Thr
-
pH 9.0, 37C
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.2
-
L-Ser
-
pH 9.0, 37C
12402
0.7
-
L-Thr
-
pH 9.0, 37C
12424
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.1
-
L-Cys
-
substrate L-Ser, pH 9.0, 37C
2.2
-
L-Cys
-
substrate L-Thr, pH 9.0, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.189
-
Q74FW6
strain DL-1
0.52
-
-
-
7.3
-
-
L-Thr
400
-
-
recombinant threonine deaminase
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
activity is much lower in quail liver than in rat liver, regardless of the nutritional state. The specific activity in the normal rat liver is 15times higher than that of the control quail group. Activities in liver of the fastened, the 1% threonine-enriched and the 5% threonine-enriched group are about 2, 1.3 and 1.5times higher, respectively, than that of the control group of quails
additional information
-
-
activity is much higher in rat liver than in quail liver, regardless of the nutritional state. The specific activity in the normal rat liver is 15times higher than that of the control quail group. The specific activity in rat liver after fasting increases by a factor of 2.3 over that of normal fed state
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.4
9.2
-
in presence of AMP
8
9
-
Tris/HCl buffer and diethanolamine buffer
8
9.5
-
in presence of 1 mM AMP
8.5
-
-
dehydratase II
8.7
-
Tetraselmis maculata
-
-
8.8
-
Chroomonas salina, Cyclotella nana
-
-
8.9
-
Anacystis marina, Hemiselmis virescens
-
-
9
9.8
-
in absence of AMP
9
-
-
in absence of AMP
9
-
Q9AXU4
activity assay
9.2
9.6
-
at 40 C and 65 C
9.4
9.6
-
-
9.5
11
-
dehydratase I
10
-
-
with L-Thr and L-Ser as substrate
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
8
-
65% of maximal activity at pH 7 and at pH 8
7.5
9.5
-
pH 7.5: about 55% of maximal activity, pH 9.5: about 85% of maximal activity
7.5
9.5
-
activity increases from pH 7.5 to pH 9.5
8.1
9.6
-
50% of maximal activity at pH 8.1 and 9.6
8.5
11
-
pH 8.5: about 30% of maximal activity, pH 11.0: about 70% of maximal activity, with L-Thr as substrate
additional information
-
P25306
the enzyme is highly active in an alkaline pH range, little or no activity is observed at pH values below 6.0
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
35
-
-
in absence of phosphate
37
-
-
in presence of 50 mM phosphate
37
-
Q9AXU4
activity assay
44
-
-
in presence of 250 mM phosphate
70
-
-
-
85
90
-
-
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
45
80
-
45C: about 25% of maximal activity, 80C: about 35% of maximal activity
60
98
-
60C: about 30% of maximal activity, 98C: about 15% of maximal activity
additional information
-
P25306
active over a wide range of temperatures, optimal enzyme activity is observed at 58C
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.7
-
-
calculated
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
primary culture
Manually annotated by BRENDA team
-
isoleucine-sensitive enzyme form occurs predominantly in younger leaves, isoleucine-insensitive enzyme form occurs predominantly in older leaves
Manually annotated by BRENDA team
additional information
-
pH for growth is in the range of pH 6.0-pH 9.0, optimal growth around pH 7.0, optimal growth conditions, overview
Manually annotated by BRENDA team
additional information
-
pH for growth is in the range of pH 6.0-pH 9.0, optimal growth around pH 7.0, optimal growth conditions, overview
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
Escherichia coli (strain K12)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
40000
-
P25306
molecular mass of processed TD2 determined by SDS-PAGE
45000
-
-
determined by gel-filtration in the absence of CMP and AMP
55000
-
P25306
determined by Western blot analysis, mature TD2
66180
-
P25306
predicted molecular mass of SlTD1
100000
115000
-
gel filtration
100000
-
-
determined by gel-filtration in the presence of CMP
106000
-
-
gel filtration
118000
-
-
gel filtration
120000
-
-
gel filtration
120000
-
-
native gradient PAGE
120000
-
-
determined by gel-filtration in the presence of AMP
140000
-
-
native PAGE, in the presence of the allosteric effector isoleucine
147000
-
-
sedimentation equilibrium ultracentrifugation
160000
-
-
gel filtration
190000
-
-
gel filtration
190000
-
-
density gradient centrifugation
200000
-
-
gel filtration
200000
-
-
Ile-insensitive enzyme form, gel filtration
201000
-
-
equilibrium sedimentation
203800
-
-
sedimentation equilibrium experiments
210000
-
-
meniscus depletion sedimentation equilibrium
210000
-
-
gel filtration
214000
-
-
meniscus depletion equilibrium sedimentation, analytical ultracentrifugation
228000
-
-
calculation from sedimentation and diffusion data
230000
-
-
gel filtration
250000
-
-
dehydratase II, gel filtration
268000
-
-
native PAGE, in the absence of allosteric effector
370000
-
-
Ile-sensitive enzyme form, gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 45000, calculated
dimer
-
2 * 55000, SDS-PAGE
dimer
-
2 * 59567, mass spectrometry, addition of isoleucine induces dimerization, tetrmerization is restored by addition of high valine concentration
tetramer
-
4 * 39000, SDS-PAGE
tetramer
-
4 * 46000, SDS-PAGE
tetramer
-
4 * 58000, SDS-PAGE
tetramer
-
4 * 32000, SDS-PAGE
tetramer
-
x * 38000, SDS-PAGE
tetramer
-
4 * 49000, SDS-PAGE
tetramer
-
4 * 57000, SDS-PAGE
tetramer
-
4 * 53000, the enzyme exists in two distinct catalytically active species: a tetramer sensitive to L-Ile inhibition and a dimer insensitive to L-Ile inhibition, SDS-PAGE
tetramer
-
4 * 49800, equilibrium sedimentation of the enzyme dialyzed against 6 M guanidine hydrochloride
tetramer
-
4 * 50000, SDS-PAGE
tetramer
-
4 * 56000, SDS-PAGE
tetramer
-
4 * 30000, SDS-PAGE
tetramer
-
4 * 46599, calculation from nucleotide sequence
tetramer
-
4 * 59800, SDS-PAGE
tetramer
-
4 * 59567, mass spectrometry
tetramer
Escherichia coli K 12
-
4 * 56000, SDS-PAGE; 4 * 57000, SDS-PAGE; x * 38000, SDS-PAGE
-
tetramer
Morganella morganii AKU 0084
-
4 * 58000, SDS-PAGE
-
dimer
Chloroflexus aurantiacus Ok-79-fl
-
2 * 55000, SDS-PAGE
-
additional information
-
the short C-terminal regulatory domain is composed of only one ACT-like subdomain
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
crystal structure at 2.8 A resolution
-
data for two crystal forms are collected to resolutions of 2.2 and 1.7 A, crystals obtainted in the presence of CMP diffract to a resolution of 3-3.5 A, in the presence of AMP poorly
-
two data sets of resolutions 2.2 A, crystal form I, and 1.7 A, crystal form II, are collected
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0
-
-
10 h, 81% loss of activity in presence of 0.05 mM Ile, stable in presence of 1 mM Ile
27
-
-
10 h, 27% loss of activity in presence of 0.05 mM Ile, stable in presence of 1 mM Ile
37
-
-
10 min, 16% loss of activity of dehydratase I and 36% loss of activity of dehydratase II, loss of activity of dehydratase I is prevented by 1 mM Ile, but that of dehydratase II is not
45
-
-
15 min, complete loss of activity in absence of phosphate, 94% loss of activity in presence of 50 mM phosphate, 49% loss of activity in presence of 250 mM phosphate
55
-
-
10 min, stable
70
-
-
1 h, 15% loss of activity
90
-
-
rapid inactivation
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
loss of activity of dehydratase I at 37 C is prevented by 1 mM Ile, but that of dehydratase II is not
-
dithiothreitol, allothreonine and pyridoxal phosphate are all required to maintain a stable form of threonine dehydratase
-
L-Ile protects the enzyme against inactivation at low temperatures
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, loss of activity after storage of more than one day
-
0-4C, stable for at least 2 months
-
0C, rapid loss of activity unless maintained in presence of Ile and potassium phosphate
-
-20C, 50% loss of activity after 3 weeks
-
-20C, no loss of activity after several weeks
-
4C, pH 7.2 or 9.0, 24 h, complete inactivation after 7 days, stable in presence of egg albumin
-
4C, little loss of activity after 50 days
-
-20C, 0.05 M potassium phosphate, pH 7.2, enzyme concentration 0.06 mg/ml, half-life: 4 weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant threonine deaminase
-
mutant strain DU-21 with an activator site-deficient enzyme form
-
using a nickel-nitrilotriacetic acid affinity column
-
using a Sephadex G-25, a DEAE-cellulose DE52, a HiLoad26/60 Superdex 200 and a HiPrep 16/10 column
P25306
partial
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
-
expression in Brevibacterium flavum
-
expression in Brevibacterium flavum; expression in Corynebacterium glutamicum
-
expression of tdcB in Corynebacterium glutamicum ATCC 21799
-
ilvA expression in Nicotiana tabaccum is effectively utilized as a selectable marker gene to identify tobacco transformants when coupled with L-O-methylthreonine as the selction agent
-
gene tcdB, phylogenetic analysis of threonine ammonia-lyases
Q74FW6
into the pRSETC vector for expression in Escherichia coli BL21DE3 pLysS cells
-
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
P25306
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
induced transcription in response to osmotic stress
-
about 500 times higher transcript levels in flowers than in leaves or roots; induced transcription in response to osmotic stress
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
Val323Ala
-
feedback inhibition by L-Ile is entirely abolished, so that the enzyme is always present in a relaxed high-activity state
additional information
-
the enzyme from the regulatory mutant CU18 is indistinguishable from the wild type enzyme in molecular weight and subunit composition
additional information
-
mutants lacking yjgF generate an isoleucine-insensitive protein
additional information
-
mutant with an activator site-deficient enzyme form, the Km for L-Thr is increased 4fold as compared with the wild type enzyme
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
molecular biology
-
in contrast to the wild-type, all four transgenic TD lines are able to tolerate high concentrations of L-O-methylthreonine. This illustrates the potential use of these mutant omr genes as dominant selectable markers in plant transformation
synthesis
-
production of poly(3-hydroxybutyrate-co-3-hydroxyvalerate) from a single unrelated carbon source via threonine biosynthesis in Escherichia coli, by overexpression of threonine deaminase, which is the key factor for providing propionyl-coenzyme A (propionyl-CoA), from different host bacteria, removal of the feedback inhibition of threonine by mutating and overexpressing the thrABC operon in Escherichia coli, and knock-out of the competitive pathways of catalytic conversion of propionyl-CoA to 3-hydroxyvaleryl-CoA. Construction of a series of strains and mutants leads to production of the poly(3-hydroxybutyrate-co-3-hydroxyvalerate) copolymer with differing monomer compositions in a modified M9 medium supplemented with 20 g/liter xylose. The largest 3-hydroxyvalerate fraction obtained in the copolymer is 17.5 mol%