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EC Tree
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.
The enzyme appears in viruses and cellular organisms
Synonyms
BsBTD1, CgBTD1, CgCTD, EC 4.2.1.16, EcBTD2, EcCTD, FgIlv1, GSU0486,
ilvA , L-TD,
more
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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
threonine deaminase/dehydratase
threonine dehydrase
-
-
-
-
threonine dehydratase/deaminase
-
-
EC 4.2.1.16
-
-
formerly
-
FgIlv1
-
GSU0486
-
ilvA
-
-
L-TDH
-
-
-
-
L-threonine deaminase
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-
-
-
TD
-
-
-
-
TD1
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-
tdcB
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-
TH
-
-
Thr ammonia-lyase
-
threonine ammonia-lyase
-
threonine ammonia-lyase
-
-
threonine ammonia-lyase
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-
Threonine deaminase
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-
-
-
Threonine deaminase
-
-
-
threonine deaminase/dehydratase
-
-
threonine deaminase/dehydratase
-
-
threonine deaminase/dehydratase
-
-
threonine dehydratase
-
-
threonine dehydratase
-
-
threonine dehydratase
-
-
threonine dehydratase
-
-
threonine dehydratase
-
-
threonine dehydratase
-
-
threonine dehydratase
-
-
threonine dehydratase
-
-
threonine dehydratase
-
-
threonine dehydratase
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-
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2-aminobut-2-enoate = 2-iminobutanoate
(1b), spontaneous
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-
-
2-iminobutanoate + H2O = 2-oxobutanoate + NH3
(1c), spontaneous
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-
-
L-threonine = 2-aminobut-2-enoate + H2O
(1a)
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-
-
L-threonine = 2-oxobutanoate + NH3
L-threonine = 2-oxobutanoate + NH3
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
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-
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L-threonine = 2-oxobutanoate + NH3
The enzyme from many sources is a pyridoxal-phosphate protein
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L-threonine = 2-oxobutanoate + NH3
(overall reaction)
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-
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elimination
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elimination
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beta-position of amino acid
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elimination
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-
alpha,beta-position of amino acid
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elimination
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-
of NH3, alpha,beta-position of amino acid
-
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
beta-chloro-L-alanine
3-chloro-2-oxopropionate + NH3
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-
?
DL-allo-cystathionine
?
-
at 20% of the activity with L-Thr
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?
L-allo-threonine
?
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-
?
L-homoserine
2-oxobutanoate + NH3 + H2O
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-
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-
?
L-Thr
2-oxobutanoate + NH3
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-
-
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?
L-threonine
2-oxobutanoate + NH3
additional information
?
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beta-chloro-L-Ala
?
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?
beta-chloro-L-Ala
?
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-
?
L-allothreonine
?
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5% of the activity L-Thr
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-
?
L-allothreonine
?
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5% of the activity L-Thr
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?
L-Cys
?
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-
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?
L-Ser
pyruvate + NH3
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?
L-Ser
pyruvate + NH3
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ir
L-Ser
pyruvate + NH3
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?
L-Ser
pyruvate + NH3
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?
L-Ser
pyruvate + NH3
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?
L-serine
pyruvate + NH3
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?
L-serine
pyruvate + NH3
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no activity
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-
?
L-serine
pyruvate + NH3
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?
L-serine
pyruvate + NH3
-
isoleucine-insensitive enzyme
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-
?
L-serine
pyruvate + NH3
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-
-
?
L-serine
pyruvate + NH3
-
6% of the activity with L-Thr
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-
?
L-serine
pyruvate + NH3
-
6% of the activity with L-Thr
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?
L-serine
pyruvate + NH3
-
45% of the activity with L-Thr
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?
L-serine
pyruvate + NH3
-
dehydratase I: 26% of the activity with L-Thr, dehydratase II: 16% of the activity with L-Thr
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?
L-serine
pyruvate + NH3
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dehydratase I: 26% of the activity with L-Thr, dehydratase II: 16% of the activity with L-Thr
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?
L-serine
pyruvate + NH3
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?
L-serine
pyruvate + NH3
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?
L-serine
pyruvate + NH3
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?
L-serine
pyruvate + NH3
-
rapid loss of activity during Ser deamination
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?
L-serine
pyruvate + NH3
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20% of the activity with L-Ser
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?
L-serine
pyruvate + NH3
-
20% of the activity with L-Ser
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?
L-serine
pyruvate + NH3
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-
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?
L-serine
pyruvate + NH3
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?
L-serine
pyruvate + NH3
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-
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?
L-serine
pyruvate + NH3
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?
L-serine
pyruvate + NH3
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-
-
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?
L-serine
pyruvate + NH3
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-
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?
L-serine
pyruvate + NH3
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-
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?
L-Thr
?
-
constitutive enzyme
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-
?
L-Thr
?
-
isoleucine-insensitive enzyme is subject to glucose-mediated catabolite repression
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?
L-Thr
?
-
isoleucine-insensitive enzyme is subject to glucose-mediated catabolite repression
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?
L-Thr
?
-
the enzyme is an important element in the flux control of Ile biosynthesis
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?
L-Thr
?
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constitutive enzyme
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-
?
L-Thr
?
-
constitutive enzyme
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?
L-Thr
?
-
first reaction of the Ile pathway
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-
?
L-Thr
?
-
inducible enzyme
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-
?
L-Thr
?
-
increase of activity under gluconeogenic conditions in adult-rat hepatocytes cultured on collagen gel/nylon mesh
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-
?
L-Thr
?
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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
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-
?
L-Thr
?
-
key enzyme in biosynthesis of Ile
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-
?
L-threonine
2-oxobutanoate + NH3
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-
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?
L-threonine
2-oxobutanoate + NH3
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-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
threonine deaminase is a key regulatory enzyme in the pathway for the biosynthesis of isoleucine, allosteric enzyme regulation model, overview
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-
?
L-threonine
2-oxobutanoate + NH3
-
-
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?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
Cyclotella nana
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-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
the enzyme catalyzes the first step in the biosynthesis pathway of isoleucine for conversion of threonine to 2-oxobutanoate
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
the enzyme catalyzes the first step in the biosynthesis pathway of isoleucine for conversion of threonine to 2-oxobutanoate
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
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
-
-
-
?
L-threonine
2-oxobutanoate + NH3
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
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
the enzyme is involved in the biosynthesis of L-isoleucine
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-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
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
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?
L-threonine
2-oxobutanoate + NH3
-
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
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
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-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
Tetraselmis maculata
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-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
additional information
?
-
GSU0486 also catalyzes the deamination of L-serine, EC 4.3.1.17
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-
?
additional information
?
-
-
GSU0486 also catalyzes the deamination of L-serine, EC 4.3.1.17
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-
?
additional information
?
-
GSU0486 also catalyzes the deamination of L-serine, EC 4.3.1.17
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-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
L-serine
pyruvate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
L-Thr
?
-
constitutive enzyme
-
-
?
L-Thr
?
-
isoleucine-insensitive enzyme is subject to glucose-mediated catabolite repression
-
-
?
L-Thr
?
-
isoleucine-insensitive enzyme is subject to glucose-mediated catabolite repression
-
-
?
L-Thr
?
-
the enzyme is an important element in the flux control of Ile biosynthesis
-
-
?
L-Thr
?
-
constitutive enzyme
-
-
?
L-Thr
?
-
constitutive enzyme
-
-
?
L-Thr
?
-
first reaction of the Ile pathway
-
-
?
L-Thr
?
-
inducible enzyme
-
-
?
L-Thr
?
-
increase of activity under gluconeogenic conditions in adult-rat hepatocytes cultured on collagen gel/nylon mesh
-
-
?
L-Thr
?
-
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
?
-
key enzyme in biosynthesis of Ile
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
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
-
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
the enzyme catalyzes the first step in the biosynthesis pathway of isoleucine for conversion of threonine to 2-oxobutanoate
-
-
?
L-threonine
2-oxobutanoate + NH3
the enzyme catalyzes the first step in the biosynthesis pathway of isoleucine for conversion of threonine to 2-oxobutanoate
-
-
?
L-threonine
2-oxobutanoate + NH3
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
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
the enzyme is involved in the biosynthesis of L-isoleucine
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
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
-
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
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
-
?
L-threonine
2-oxobutanoate + NH3
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pyridoxamine 5'-phosphate
-
reactivates after dissociation of the coenzyme
ADP
-
activates
ADP
-
no stimulation by ADP
AMP
-
activates
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
required
pyridoxal 5'-phosphate
-
required
pyridoxal 5'-phosphate
-
required
pyridoxal 5'-phosphate
-
required
pyridoxal 5'-phosphate
-
contains 4 mol of pyridoxal 5'-phosphate per mol of enzyme
pyridoxal 5'-phosphate
-
contains 4 mol of pyridoxal 5'-phosphate per mol of enzyme
pyridoxal 5'-phosphate
-
contains 4 mol of pyridoxal 5'-phosphate per mol of enzyme
pyridoxal 5'-phosphate
-
activates
pyridoxal 5'-phosphate
dependent on
pyridoxal 5'-phosphate
-
tightly bound
pyridoxal 5'-phosphate
-
cofactor
pyridoxal 5'-phosphate
-
cofactor
pyridoxal 5'-phosphate
-
cofactor
pyridoxal 5'-phosphate
-
cofactor
pyridoxal 5'-phosphate
-
cofactor
pyridoxal 5'-phosphate
-
cofactor
pyridoxal 5'-phosphate
-
cofactor
pyridoxal 5'-phosphate
-
contains 2 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
-
contains 2 mol of pyridoxal 5'-phosphate per mol of enzyme
pyridoxal 5'-phosphate
-
enzyme contains 1 mol of pyridoxal 5'-phosphate per 56000 Da subunit
pyridoxal 5'-phosphate
-
Km: 0.000682 mM
pyridoxal 5'-phosphate
-
reactivates after dissociation of the coenzyme
pyridoxal 5'-phosphate
-
Km: 0.00028 mM
pyridoxal 5'-phosphate
-
1 mol per monomer
pyridoxal 5'-phosphate
-
1 molecule per monomer
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ca2+
50 mM, 1.7fold activation
Mg2+
50 mM, 1.6fold activation
Rb+
-
can partially replace K+ in activation
additional information
-
no requirement for divalent cations
K+
-
3fold increase in activity, half-maximal activation at 3.1 mM
K+
50 mM, 1.5fold activation
Li+
-
2.8fold increase in activity
Li+
50 mM, 1.5fold activation
Na+
-
1.7fold increase in activity
Na+
50 mM, 1.5fold activation
NH4+
-
stimulates
NH4+
50 mM, 1.75fold activation
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
L-Cycloserine
powerful suicide inactivator that generates a covalent pyridoxal 5'-phosphate-isoxazole complex
Mn2+
50 mM, 50% loss of activity
Na-cholatemethyl ester
-
-
p-chloromercuriphenyl sulfonate
2,2'-dithiodipyridine
-
-
2,2'-dithiodipyridine
-
-
2,2'-dithiodipyridine
Cyclotella nana
-
-
2,2'-dithiodipyridine
-
-
2,2'-dithiodipyridine
-
-
2,2'-dithiodipyridine
-
-
2,2'-dithiodipyridine
Tetraselmis maculata
-
-
2-oxobutanoate
-
20 mM, about 50% inhibition. Inhibition is not reversed by AMP
Cys
-
-
dithiothreitol
-
-
glyoxylate
-
20 mM, about 50% inhibition. Inhibition is not reversed by AMP
hydrazine
-
-
hydrazine
Cyclotella nana
-
-
hydrazine
Tetraselmis maculata
-
-
hydroxylamine
-
-
hydroxylamine
Cyclotella nana
-
reversed by pyridoxal 5'-phosphate
hydroxylamine
Tetraselmis maculata
-
-
Ile
-
reversed by low concentrations of L-Val
Ile
-
50% inhibition at 0.14 mM Ile, 98% inhibition at 1 mM Ile
Ile
-
2 enzyme forms: an isoleucine-sensitive enzyme form and and isoleucine-insensitive form, pH-dependence of inhibition
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
-
0.06 mM, 50% inhibition
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
-
negative allosteric effector
Ile
-
biodegradative enzyme is feedback-resistant
Ile
-
inhibition of isoleucine can be reversed by valine
Ile
-
dehydratase I, 50% inhibition at 0.35 mM
Ile
-
more sensitive at 40 C than at 65 C
Ile
-
2 different forms: one enzyme form is sensitive to inhibition by Ile, the other form is insensitive to inhibition by Ile
Ile
-
feed-back inhibition; HgCl2 treated enzyme is less sensitive; L-Val partially reverses inhibition
Ile
-
feed-back inhibition
iodoacetamide
-
-
iodoacetamide
Cyclotella nana
-
weak
iodoacetamide
Tetraselmis maculata
-
weak
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
-
end product inhibition, reversed by valine, the short C-terminal regulatory domain is composed of one ACT-like subdomain, which binds isoleucine and valine
isoleucine
-
feedback inhibition
isoniazid
-
-
isoniazid
Cyclotella nana
-
-
isoniazid
Tetraselmis maculata
-
-
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-isoleucine
less than 2% activity remains after addition of 0.5 mM L-isoleucine
L-isoleucine
-
allosteric inhibition
L-Val
-
competitive
L-Val
-
slight inhibition
Leu
-
-
Leu
-
dehydratase I, 6 mM, 50% inhibition
methoxylamine
-
-
methoxylamine
Cyclotella nana
-
-
methoxylamine
Tetraselmis maculata
-
-
NaBH4
-
-
NEM
-
-
NEM
Tetraselmis maculata
-
-
NSD-1055
-
-
NSD-1055
Cyclotella nana
-
-
NSD-1055
Tetraselmis maculata
-
-
p-chloromercuriphenyl sulfonate
-
-
p-chloromercuriphenyl sulfonate
-
-
p-chloromercuriphenyl sulfonate
Cyclotella nana
-
-
p-chloromercuriphenyl sulfonate
-
-
p-chloromercuriphenyl sulfonate
-
-
p-chloromercuriphenyl sulfonate
-
-
p-chloromercuriphenyl sulfonate
Tetraselmis maculata
-
-
PCMB
-
-
phenylhydrazine
-
reversed by pyridoxal 5'-phosphate
phenylhydrazine
Cyclotella nana
-
reversed by pyridoxal 5'-phosphate
pyruvate
-
20 mM, about 50% inhibition. Inhibition is not reversed by AMP
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
Semicarbazide
-
-
Semicarbazide
Cyclotella nana
-
-
Semicarbazide
Tetraselmis maculata
-
-
Ser
-
L-Ser, competitive with respect to L-Thr
additional information
-
feedback-inhibition of threonine deaminase by branched-chain amino acids
-
additional information
TcdB is not inhibited by isoleucine
-
additional information
-
TcdB is not inhibited by isoleucine
-
additional information
-
feedback-inhibition of threonine deaminase by branched-chain amino acids
-
additional information
-
feedback-inhibition of threonine deaminase by branched-chain amino acids
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
isoleucine
-
activation below 0.01 mM, strong inhibition above, 50% inhibition at 0.064 mM
NH4+
-
2.1fold increase in activity
L-Val
-
activates
L-valine
-
-
L-valine
activator, (0-10 mM) leads to a nearly 50% increase in MsIlvA activity
phosphate
-
increases activity
phosphate
-
increases activity
phosphate
-
maximal stimulation at 200 mM
phosphate
-
increases activity
phosphate
-
increases activity
phosphate
-
increases activity
phosphate
-
increases activity
phosphate
-
increases activity
phosphate
-
increases activity
phosphate
-
increases activity
phosphate
-
increases activity
phosphate
-
increases activity
phosphate
-
increases activity
phosphate
-
increases activity
phosphate
-
increases activity
additional information
-
threonine aldolase mutations increase substrate availability for threonine deaminase
-
additional information
-
insensitive to the allosteric activation by AMP or CMP
-
additional information
-
dehydratase I and II: not affected by adenylates
-
additional information
-
no activation by AMP, ADP and ATP
-
additional information
the plant activates threonine deaminase in tissues attacked by herbivores
-
additional information
-
the plant activates threonine deaminase in tissues attacked by herbivores
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Abscess
Enzymatically active Peptostreptococcus magnus: association with site of infection.
Carcinoma, Hepatocellular
Metabolic adaptations in rat hepatomas. V. Reciprocal relationship between threonine dehydrase and glucose-6-phosphate dehydrogenase.
Carcinoma, Hepatocellular
[Characteristics of L-threonine- and L-serine dehydratases from mouse liver and spontaneous hepatomas]
Cardiovascular Diseases
Effect of alpha-ketobutyrate on microvascular thickness in the diabetic rat kidney.
Dehydration
Adaptive evolution of threonine deaminase in plant defense against insect herbivores.
Dehydration
Inhibition of Threonine Dehydratase Is Herbicidal.
Dehydration
Mechanism of the inactivation of threonine dehydratase during the dehydration of serine.
Diabetic Foot
Enzymatically active Peptostreptococcus magnus: association with site of infection.
Hypersensitivity
Isoleucine auxotrophy due to feedback hypersensitivity of biosynthetic threonine deaminase.
Infections
Enzymatically active Peptostreptococcus magnus: association with site of infection.
Infections
SP0454, a putative threonine dehydratase, is required for pneumococcal virulence in mice.
Keratoconjunctivitis
[Correlation between biochemical features and pathogenicity of Shigella. IV. Threonine deaminase of Shigella strains producing and not producing keratoconjunctivitis in guinea pigs]
Leukemia
Effects of threonine deaminase on growth and viability of mammalian cells in tissue culture and its selective cytotoxicity toward leukemia cells.
Pneumococcal Infections
SP0454, a putative threonine dehydratase, is required for pneumococcal virulence in mice.
Scrapie
Genomic and experimental evidence for multiple metabolic functions in the RidA/YjgF/YER057c/UK114 (Rid) protein family.
Sick Sinus Syndrome
Indirectly estimated sinoatrial conduction time by the atrial premature stimulus technique: patterns of error and the degree of associated inaccuracy as assessed by direct sinus node electrography.
Sick Sinus Syndrome
[Evaluation of sinoatrial conduction time by recording the sinus node potential. Comparison with indirect methods of evaluation]
Starvation
Regulation of isoleucine-valine biosynthesis in Saccharomyces cerevisiae.
Starvation
The energy-yielding reactions of Peptococcus prévotii, their behaviour on starvation and the role and regulation of threonine dehydratase.
threonine ammonia-lyase deficiency
Threonine dehydratase deficiency: a probable cause of non-ketotic hyperglycinaemia.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3.01
beta-chloro-L-alanine
pH 8.0, 30°C
2.86
L-allo-threonine
pH 8.0, 30°C
additional information
additional information
-
Monod-Wyman-Changeux symmetrical model analysis of steady-state kinetics for the wild-type and four mutant enzymes
-
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, 37°C
30.3
L-Ser
-
in absence of AMP
40
L-Ser
-
in absence of AMP
80
L-Ser
-
mutant strain DU-21
90
L-Ser
-
wild type enzyme
3
L-serine
processed TD2
106.3
L-serine
pH 8.0, 30°C
0.25
L-Thr
-
-
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
4.5
L-Thr
-
wild type enzyme
7.3
L-Thr
-
pH 9.0, 37°C
11
L-Thr
-
in presence of AMP
13
L-Thr
-
dehydratase II
19
L-Thr
-
mutant strain DU-21
20
L-Thr
-
Ile-insensitive enzyme
21.3
L-Thr
-
Ile-sensitive enzyme
24
L-Thr
-
in absence of AMP
91
L-Thr
-
in absence of AMP
1.66
L-threonine
pH 8.0, 30°C
2.3
L-threonine
processed TD2
3 - 3.5
L-threonine
pH 7.5, 30°C, mutant enzyme G323D/R449C
14.5
L-threonine
pH 7.5, 30°C, wild-type enzyme
16
L-threonine
-
in the presence of 5 mM AMP
26.2
L-threonine
pH 7.5, 30°C, mutant enzyme G323D/F510L/T344A
26.4
L-threonine
pH 7.5, 30°C, mutant enzyme G323D/F510L
26.9
L-threonine
pH 7.5, 30°C, mutant enzyme G323D/F510L/T344A/R449C
27.1
L-threonine
pH 7.5, 30°C, mutant enzyme G323D/F510L/R449C
28.3
L-threonine
pH 7.5, 30°C, mutant enzyme F510L
30.1
L-threonine
pH 7.5, 30°C, mutant enzyme A14T/G323D
32
L-threonine
-
in the presence of 5 mM CMP
32.5
L-threonine
pH 7.5, 30°C, mutant enzyme A14T
32.8
L-threonine
pH 7.5, 30°C, mutant enzyme R449C
33.3
L-threonine
pH 7.5, 30°C, mutant enzyme T344A
33.6
L-threonine
pH 7.5, 30°C, mutant enzyme G323D
33.7
L-threonine
pH 7.5, 30°C, mutant enzyme G323D/T344A
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
27.15
beta-chloro-L-alanine
pH 8.0, 30°C
5.69
L-allo-threonine
pH 8.0, 30°C
32.59
L-serine
pH 8.0, 30°C
3
L-Ser
-
pH 9.0, 37°C
5.2
L-Thr
-
pH 9.0, 37°C
9.42
L-threonine
pH 8.0, 30°C
1230
L-threonine
pH 7.5, 30°C, mutant enzyme F510L
1256
L-threonine
pH 7.5, 30°C, mutant enzyme T344A
1261
L-threonine
pH 7.5, 30°C, mutant enzyme A14T
1273
L-threonine
pH 7.5, 30°C, mutant enzyme R449C
1283
L-threonine
pH 7.5, 30°C, mutant enzyme G323D/F510L
1298
L-threonine
pH 7.5, 30°C, mutant enzyme G323D/F510L/R449C
1301
L-threonine
pH 7.5, 30°C, mutant enzyme G323D/F510L/T344A/R449C
1309
L-threonine
pH 7.5, 30°C, mutant enzyme G323D/F510L/T344A
1312
L-threonine
pH 7.5, 30°C, mutant enzyme G323D/R449C
1369
L-threonine
pH 7.5, 30°C, mutant enzyme A14T/G323D
1394
L-threonine
pH 7.5, 30°C, mutant enzyme G323D/T344A
1398
L-threonine
pH 7.5, 30°C, mutant enzyme G323D
1414
L-threonine
pH 7.5, 30°C, wild-type enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
9.02
beta-chloro-L-alanine
pH 8.0, 30°C
1.99
L-allo-threonine
pH 8.0, 30°C
0.2
L-Ser
-
pH 9.0, 37°C
0.03
L-serine
pH 8.0, 30°C
0.7
L-Thr
-
pH 9.0, 37°C
5.7
L-threonine
pH 8.0, 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.06
Ile
-
-
1.1
L-Cys
-
substrate L-Ser, pH 9.0, 37°C
2.2
L-Cys
-
substrate L-Thr, pH 9.0, 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.009
Ile
Escherichia coli
-
pH 7.5, 30°C, mutant E442A
0.037
Ile
Escherichia coli
-
pH 7.5, 30°C, mutant G350E
0.067
Ile
Escherichia coli
-
pH 7.5, 30°C, wild-type
0.162
Ile
Escherichia coli
-
pH 7.5, 30°C, mutant G445E
2.32
Ile
Escherichia coli
-
pH 7.5, 30°C, mutant F352A
2.86
Ile
Escherichia coli
-
pH 7.5, 30°C, mutant E347F
3.27
Ile
Escherichia coli
-
pH 7.5, 30°C, mutant I460F
6.99
Ile
Escherichia coli
-
pH 7.5, 30°C, mutant R362F
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
100.2
pH 7.5, 30°C, mutant enzyme G323D/R449C
100.4
pH 7.5, 30°C, mutant enzyme A14T/G323D
101
pH 7.5, 30°C, mutant enzyme G323D/F510L/R449C
104.6
pH 7.5, 30°C, mutant enzyme G323D
108
pH 7.5, 30°C, wild-type enzyme
400
-
recombinant threonine deaminase
68.5
pH 7.5, 30°C, mutant enzyme A14T
77.4
pH 7.5, 30°C, mutant enzyme T344A
78.8
pH 7.5, 30°C, mutant enzyme F510L
89.5
pH 7.5, 30°C, mutant enzyme R449C
99.4
pH 7.5, 30°C, mutant enzyme G323D/F510L
99.5
pH 7.5, 30°C, mutant enzyme G323D/F510L/T344A
99.5
pH 7.5, 30°C, mutant enzyme G323D/F510L/T344A/R449C
99.5
pH 7.5, 30°C, mutant enzyme G323D/T344A
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
-
-
additional information
-
-
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
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
10
-
with L-Thr and L-Ser as substrate
7.4 - 9.2
-
in presence of AMP
8 - 9.5
-
in presence of 1 mM AMP
8.7
Tetraselmis maculata
-
-
9 - 9.8
-
in absence of AMP
7.5
-
assay at
8
-
-
8 - 9
-
-
8 - 9
-
Tris/HCl buffer and diethanolamine buffer
8.5
-
dehydratase II
8.8
-
-
8.9
-
-
9
-
in absence of AMP
9.2 - 9.6
-
-
9.2 - 9.6
-
at 40 C and 65 C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
6.8 - 8.9
pH has no significant effect on activity
7 - 8
-
65% of maximal activity at pH 7 and at pH 8
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
the enzyme is highly active in an alkaline pH range, little or no activity is observed at pH values below 6.0
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
35
-
in absence of phosphate
44
-
in presence of 250 mM phosphate
22
-
assay at
30
-
assay at
37
-
in presence of 50 mM phosphate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
45 - 80
-
45°C: about 25% of maximal activity, 80°C: about 35% of maximal activity
60 - 98
-
60°C: about 30% of maximal activity, 98°C: about 15% of maximal activity
additional information
active over a wide range of temperatures, optimal enzyme activity is observed at 58°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
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brenda
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SwissProt
brenda
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brenda
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brenda
Japanese quail, male
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brenda
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brenda
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brenda
Cyclotella nana
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brenda
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brenda
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brenda
dehydratase I and dehydratase II
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brenda
dehydratase I and dehydratase II
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brenda
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UniProt
brenda
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UniProt
brenda
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brenda
strain DL-1, ATCC 51573, gene GSU0486 or tcdB
UniProt
brenda
strain DL-1, ATCC 51573, gene GSU0486 or tcdB
UniProt
brenda
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brenda
biosynthetic threonine deaminase
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brenda
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brenda
biosynthetic threonine deaminase
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brenda
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UniProt
brenda
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SwissProt
brenda
-
-
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brenda
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-
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brenda
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brenda
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-
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brenda
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-
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brenda
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brenda
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brenda
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brenda
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brenda
gene ilvA
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brenda
gene ilvA
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
i.e. Agmenellum quadruplicatum
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brenda
Tetraselmis maculata
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brenda
X-1
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brenda
X-1
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brenda
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brenda
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brenda
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brenda
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brenda
2 enzyme forms: an isoleucine-sensitive enzyme form and and an isoleucine-insensitive form
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brenda
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brenda
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SwissProt
brenda
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210823 , 210832 , 210833 , 210836 , 210842 , 210847 , 210856 , 649402 , 653575 , 729066 , 730759 -
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brenda
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SwissProt
brenda
a genetically derepressed mutant strain of Escherichia coli K12
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brenda
ATCC 14948
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brenda
biodegradative threonine dehydratase
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brenda
biosynthetic threonine deaminase
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brenda
ilvA mutant encoding an enzyme that is resistant to feedback inhibition by L-Ile
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brenda
regulatory mutant CU18
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brenda
the enzyme exists in two distinct catalytically active species: a tetramer sensitive to L-Ile inhibition and a dimer insensitive to L-Ile inhibition
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brenda
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brenda
biosynthetic threonine deaminase
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brenda
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brenda
biodegradative threonine dehydratase
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brenda
mutant with an activator site-deficient enzyme form
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brenda
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brenda
ATCC 25419
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brenda
strain IHr313, strain 149 lacks L-threonine dehydratase
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brenda
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Uniprot
brenda
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brenda
2 different forms: one enzyme form is sensitive to inhibition by Ile, the other form is insensitive to inhibition by Ile
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brenda
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primary culture
brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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isoleucine-sensitive enzyme form occurs predominantly in younger leaves, isoleucine-insensitive enzyme form occurs predominantly in older leaves
brenda
-
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brenda
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brenda
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brenda
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brenda
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brenda
additional information
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pH for growth is in the range of pH 6.0-pH 9.0, optimal growth around pH 7.0, optimal growth conditions, overview
brenda
additional information
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pH for growth is in the range of pH 6.0-pH 9.0, optimal growth around pH 7.0, optimal growth conditions, overview
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brenda
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brenda
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brenda
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brenda
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physiological function
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SP0454 contributes to virulence and colonization
malfunction
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reduced threoinine deaminase causes severe growth defects
malfunction
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reduced threoinine deaminase causes severe growth defects
malfunction
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sp0454 deletion mutant is less virulent in a murine intranasal infection model
malfunction
the FgILV1 deletion mutant DELTAFgIlv1-3 is unable to grow on minimal medium or fructose gelatin agar which lacks isoleucine. The mutant displays decreased virulence on wheat heads and a low level of deoxynivalenol production in wheat kernels. Deletion of FgILV1 also causes defects in conidial formation and germination
malfunction
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the FgILV1 deletion mutant DELTAFgIlv1-3 is unable to grow on minimal medium or fructose gelatin agar which lacks isoleucine. The mutant displays decreased virulence on wheat heads and a low level of deoxynivalenol production in wheat kernels. Deletion of FgILV1 also causes defects in conidial formation and germination
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metabolism
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involved in methionine metabolism, plays a predominant role in isoleucine synthesis
metabolism
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involved in methionine metabolism, plays a predominant role in isoleucine synthesis
metabolism
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involved in methionine metabolism, plays a predominant role in isoleucine synthesis
metabolism
the enzyme catalyzes the first step in the biosynthesis pathway of isoleucine for conversion of threonine to 2-oxobutanoate. FgIlv1 is an essential component in isoleucine biosynthesis and is required for various cellular processes including mycelial and conidial morphogenesis, deoxynivalenol biosynthesis, and full virulence in Fusarium graminearum
metabolism
the enzyme is involved in the biosynthesis of L-isoleucine
metabolism
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the enzyme catalyzes the first step in the biosynthesis pathway of isoleucine for conversion of threonine to 2-oxobutanoate. FgIlv1 is an essential component in isoleucine biosynthesis and is required for various cellular processes including mycelial and conidial morphogenesis, deoxynivalenol biosynthesis, and full virulence in Fusarium graminearum
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100000
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determined by gel-filtration in the presence of CMP
100000 - 115000
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gel filtration
140000
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native PAGE, in the presence of the allosteric effector isoleucine
147000
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sedimentation equilibrium ultracentrifugation
201000
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equilibrium sedimentation
203800
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sedimentation equilibrium experiments
214000
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meniscus depletion equilibrium sedimentation, analytical ultracentrifugation
228000
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calculation from sedimentation and diffusion data
250000
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dehydratase II, gel filtration
268000
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native PAGE, in the absence of allosteric effector
30000
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4 * 30000, SDS-PAGE
370000
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Ile-sensitive enzyme form, gel filtration
38000
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x * 38000, SDS-PAGE
39000
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4 * 39000, SDS-PAGE
40000
molecular mass of processed TD2 determined by SDS-PAGE
46000
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4 * 46000, SDS-PAGE
46599
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4 * 46599, calculation from nucleotide sequence
49000
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4 * 49000, SDS-PAGE
49800
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4 * 49800, equilibrium sedimentation of the enzyme dialyzed against 6 M guanidine hydrochloride
50000
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4 * 50000, SDS-PAGE
53000
-
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
56000
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4 * 56000, SDS-PAGE
57000
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4 * 57000, SDS-PAGE
58000
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4 * 58000, SDS-PAGE
59800
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4 * 59800, SDS-PAGE
66180
predicted molecular mass of SlTD1
120000
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120000
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native gradient PAGE
120000
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determined by gel-filtration in the presence of AMP
190000
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gel filtration
190000
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density gradient centrifugation
200000
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gel filtration
200000
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Ile-insensitive enzyme form, gel filtration
210000
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210000
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meniscus depletion sedimentation equilibrium
32000
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32000
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4 * 32000, SDS-PAGE
36000
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determined by SDS-PAGE
36000
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x * 36000, SDS-PAGE
45000
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determined by gel-filtration in the absence of CMP and AMP
45000
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x * 45000, calculated
55000
determined by Western blot analysis, mature TD2
55000
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2 * 55000, SDS-PAGE
59567
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2 * 59567, mass spectrometry, addition of isoleucine induces dimerization, tetrmerization is restored by addition of high valine concentration
59567
-
4 * 59567, mass spectrometry
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?
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x * 45000, calculated
additional information
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the short C-terminal regulatory domain is composed of only one ACT-like subdomain
dimer
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2 * 59567, mass spectrometry, addition of isoleucine induces dimerization, tetrmerization is restored by addition of high valine concentration
dimer
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2 * 55000, SDS-PAGE
dimer
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2 * 55000, SDS-PAGE
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tetramer
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4 * 39000, SDS-PAGE
tetramer
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4 * 59567, mass spectrometry
tetramer
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4 * 59800, SDS-PAGE
tetramer
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4 * 46000, SDS-PAGE
tetramer
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4 * 46599, calculation from nucleotide sequence
tetramer
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4 * 50000, SDS-PAGE
tetramer
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x * 38000, SDS-PAGE
tetramer
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4 * 57000, SDS-PAGE
tetramer
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4 * 56000, SDS-PAGE
tetramer
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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
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4 * 49800, equilibrium sedimentation of the enzyme dialyzed against 6 M guanidine hydrochloride
tetramer
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x * 38000, SDS-PAGE
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tetramer
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4 * 57000, SDS-PAGE
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tetramer
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4 * 56000, SDS-PAGE
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tetramer
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4 * 49000, SDS-PAGE
tetramer
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4 * 58000, SDS-PAGE
tetramer
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4 * 32000, SDS-PAGE
tetramer
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4 * 58000, SDS-PAGE
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tetramer
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x * 36000, SDS-PAGE
tetramer
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in the complex with CMP
tetramer
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4 * 30000, SDS-PAGE
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crystal structure at 2.8 A resolution
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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
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two data sets of resolutions 2.2 A, crystal form I, and 1.7 A, crystal form II, are collected
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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
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0
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10 h, 81% loss of activity in presence of 0.05 mM Ile, stable in presence of 1 mM Ile
27
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10 h, 27% loss of activity in presence of 0.05 mM Ile, stable in presence of 1 mM Ile
37
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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
39
15 min, 50% loss of activity, wild-type enzyme
41
15 min, 50% loss of activity, mutant enzyme A14T
41.2
15 min, 50% loss of activity, mutant enzyme R449C
44.8
15 min, 50% loss of activity, mutant enzyme F510L
45
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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
46.2
15 min, 50% loss of activity, mutant enzyme G323D
47.1
15 min, 50% loss of activity, mutant enzyme G323D/T344A
52.4
15 min, 50% loss of activity, mutant enzyme G323D/F510L/R449C
52.5
15 min, 50% loss of activity, mutant enzyme G323D/F510L
70
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1 h, 15% loss of activity
42
15 min, 50% loss of activity, mutant enzyme T344A
42
half-life: 10 min (wild-type enzyme), 210 min (mutant enzyme G323D/F510L/T344A), 14 min (mutant enzyme A14T), 19 min (mutant enzyme T344A), 15 min (mutant enzyme R449C), 57 min (mutant enzyme G323D), 44 min (mutant enzyme F510L), 54 min (mutant enzyme A14T/G323D and mutant enzyme G323D/R449C), 61 min (mutant enzyme G323D/T344A), 201 min (mutant enzyme G323D/F510L), 200 min (mutant enzyme G323D/F510L/R449C), 211 min (mutant enzyme G323D/F510L/T344A/R449C)
43
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T50: 43°C
46
15 min, 50% loss of activity, mutant enzyme A14T/G323D
46
15 min, 50% loss of activity, mutant enzyme G323D/R449C
47
-
T50: 47°C
53
15 min, 50% loss of activity, mutant enzyme G323D/F510L/T344A
55
-
T50: 55°C
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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
-
loss of activity of dehydratase I at 37 C is prevented by 1 mM Ile, but that of dehydratase II is not
-
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-20°C, 0.05 M potassium phosphate, pH 7.2, enzyme concentration 0.06 mg/ml, half-life: 4 weeks
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-20°C, 50% loss of activity after 3 weeks
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-20°C, no loss of activity after several weeks
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0-4°C, stable for at least 2 months
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0°C, rapid loss of activity unless maintained in presence of Ile and potassium phosphate
-
4°C, little loss of activity after 50 days
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4°C, loss of activity after storage of more than one day
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4°C, pH 7.2 or 9.0, 24 h, complete inactivation after 7 days, stable in presence of egg albumin
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mutant strain DU-21 with an activator site-deficient enzyme form
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recombinant threonine deaminase
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using a nickel-nitrilotriacetic acid affinity column
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using a Sephadex G-25, a DEAE-cellulose DE52, a HiLoad26/60 Superdex 200 and a HiPrep 16/10 column
using Ni-NTA chromatography
-
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partial
-
using Ni-NTA chromatography
-
using Ni-NTA chromatography
-
using Ni-NTA chromatography
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using Ni-NTA chromatography
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using Ni-NTA chromatography
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using Ni-NTA chromatography
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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
expressed in Escherichia coli as a His-tagged fusion protein
expression in Brevibacterium flavum
-
expression in Corynebacterium glutamicum
-
expression in Escherichia coli
expression in Escherichia coli BL21 (DE3)
expression of tdcB in Corynebacterium glutamicum ATCC 21799
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expression of the mutant enzyme G323D/F510L/T344A in Escherichia coli BL21(DE3)
gene tcdB, phylogenetic analysis of threonine ammonia-lyases
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
-
into the pRSETC vector for expression in Escherichia coli BL21DE3 pLysS cells
-
-
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expressed in Escherichia coli as a His-tagged fusion protein
-
expressed in Escherichia coli as a His-tagged fusion protein
-
expressed in Escherichia coli as a His-tagged fusion protein
-
expressed in Escherichia coli as a His-tagged fusion protein
-
expressed in Escherichia coli as a His-tagged fusion protein
-
expressed in Escherichia coli as a His-tagged fusion protein
-
expression in Escherichia coli
-
expression in Escherichia coli
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