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Information on EC 4.3.1.19 - threonine ammonia-lyase and Organism(s) Corynebacterium glutamicum and UniProt Accession Q04513

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EC Tree
     4 Lyases
         4.3 Carbon-nitrogen lyases
             4.3.1 Ammonia-lyases
                4.3.1.19 threonine ammonia-lyase
IUBMB Comments
Most enzymes that catalyse this reaction are pyridoxal-phosphate-dependent, although some enzymes contain an iron-sulfur cluster instead. The reaction catalysed by both types of enzymes involves the initial elimination of water to form an enamine intermediate (hence the enzyme's original classification as EC 4.2.1.16, threonine dehydratase), followed by tautomerization to an imine form and hydrolysis of the C-N bond [3,5]. The latter reaction, which can occur spontaneously, is also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase . The enzymes from a number of sources also act on L-serine, cf. EC 4.3.1.17, L-serine ammonia-lyase.
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This record set is specific for:
Corynebacterium glutamicum
UNIPROT: Q04513
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Word Map
The taxonomic range for the selected organisms is: Corynebacterium glutamicum
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide(Overall reactions are displayed. Show all >>)
Synonyms
threonine deaminase, threonine dehydratase, sactd, threonine ammonia-lyase, sp0454, fgilv1, l-tdh, threonine dehydratase/deaminase, threonine deaminase/dehydratase, threonine dehydrase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
threonine dehydratase
-
L-TDH
-
-
-
-
L-threonine deaminase
-
-
-
-
L-threonine dehydratase
-
-
-
-
TD
-
-
-
-
TDH
-
-
-
-
Threonine deaminase
-
-
-
-
threonine dehydrase
-
-
-
-
threonine dehydratase
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Deamination
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
L-threonine ammonia-lyase (2-oxobutanoate-forming)
Most enzymes that catalyse this reaction are pyridoxal-phosphate-dependent, although some enzymes contain an iron-sulfur cluster instead. The reaction catalysed by both types of enzymes involves the initial elimination of water to form an enamine intermediate (hence the enzyme's original classification as EC 4.2.1.16, threonine dehydratase), followed by tautomerization to an imine form and hydrolysis of the C-N bond [3,5]. The latter reaction, which can occur spontaneously, is also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase [5]. The enzymes from a number of sources also act on L-serine, cf. EC 4.3.1.17, L-serine ammonia-lyase.
CAS REGISTRY NUMBER
COMMENTARY hide
9024-34-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-Thr
?
show the reaction diagram
-
the enzyme is an important element in the flux control of Ile biosynthesis
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-Thr
?
show the reaction diagram
-
the enzyme is an important element in the flux control of Ile biosynthesis
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8500
-
pH 8, 22°C
89000
-
pH 8, 22°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
46599
-
4 * 46599, calculation from nucleotide sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
-
4 * 46599, calculation from nucleotide sequence
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
-
feedback inhibition by L-Ile is entirely abolished, so that the enzyme is always present in a relaxed high-activity state
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
using Ni-NTA chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli BL21 (DE3)
expressed in Escherichia coli as a His-tagged fusion protein
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
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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%
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sahm, H.; Eggeling, L.; Eikmanns, B.; Kraemer, R.
Construction of L-lysine-, L-threonine-, and L-isoleucine-overproducing strains of Corynebacterium glutamicum
Ann. N. Y. Acad. Sci.
782
25-39
1996
Corynebacterium glutamicum
Manually annotated by BRENDA team
Guillouet, S.; Rodal, A.A.; An, G.H.; Lessard, P.A.; Sinskey, A.J.
Expression of the Escherichia coli catabolic threonine dehydratase in Corynebacterium glutamicum and its effect on isoleucine production
Appl. Environ. Microbiol.
65
3100-3107
1999
Corynebacterium glutamicum, Escherichia coli
Manually annotated by BRENDA team
Moeckel, B.; Eggeling, L.; Sahm, H.
Functional and structural analyses of threonine dehydratase from Corynebacterium glutamicum
J. Bacteriol.
174
8065-8072
1992
Corynebacterium glutamicum
Manually annotated by BRENDA team
Morbach, S.; Kelle, R.; Winkels, S.; Sahm, H.; Eggeling, L.
Engineering the homoserine dehydrogenase and threonine dehydratase control points to analyse flux towards L-isoleucine in Corynebacterium glutamicum
Appl. Microbiol. Biotechnol.
45
612-620
1996
Corynebacterium glutamicum
-
Manually annotated by BRENDA team
Chen, Q.; Wang, Q.; Wei, G.; Liang, Q.; Qi, Q.
Production in Escherichia coli of poly(3-hydroxybutyrate-co-3-hydroxyvalerate) with differing monomer compositions from unrelated carbon sources
Appl. Environ. Microbiol.
77
4886-4893
2011
Corynebacterium glutamicum
Manually annotated by BRENDA team
Yu, X.; Li, Y.; Wang, X.
Molecular evolution of threonine dehydratase in bacteria
PLoS ONE
8
e80750
2013
Bacillus subtilis, Corynebacterium glutamicum, Escherichia coli, Staphylococcus aureus, Pseudomonas putida, Streptomyces griseus
Manually annotated by BRENDA team
Guo, Y.; Xu, J.; Han, M.; Zhang, W.
Generation of mutant threonine dehydratase and its effects on isoleucine synthesis in Corynebacterium glutamicum
World J. Microbiol. Biotechnol.
31
1369-1377
2015
Corynebacterium glutamicum (Q04513), Corynebacterium glutamicum, Corynebacterium glutamicum ATCC 13032 (Q04513)
Manually annotated by BRENDA team