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Information on EC 4.2.3.1 - threonine synthase and Organism(s) Thermus thermophilus and UniProt Accession P83823

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.3 Acting on phosphates
                4.2.3.1 threonine synthase
IUBMB Comments
A pyridoxal-phosphate protein.
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This record set is specific for:
Thermus thermophilus
UNIPROT: P83823
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Word Map
The taxonomic range for the selected organisms is: Thermus thermophilus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
threonine synthase, threonine synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthase, threonine
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threonine synthetase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
O-phospho-L-homoserine + H2O = L-threonine + phosphate
show the reaction diagram
the phosphate ion released from O-phospho-L-homoserine by gamma-elimination acts as the base catalyst for the addition of water at Cbeta of the alpha-aminocrotonate aldimine, thereby providing the basis of the reaction specificity. The phosphate ion also accelerates the protonation/deprotonation at Cgamma
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
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SYSTEMATIC NAME
IUBMB Comments
O-phospho-L-homoserine phosphate-lyase (adding water; L-threonine-forming)
A pyridoxal-phosphate protein.
CAS REGISTRY NUMBER
COMMENTARY hide
9023-97-6
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
O-phospho-L-homoserine + H2O
L-threonine + phosphate
show the reaction diagram
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-
?
L-vinylglycine + phosphate + H2O
L-threonine + phosphate
show the reaction diagram
in the presence of phosphate, L-threonine is formed with kcat and reaction specificity comparable with those when O-phospho-L-homoserine is used as the substrate. In the absence of phosphate or when sulfate is used in place of phosphate, only the side reaction product, alpha-ketobutyrate, is formed. Compared with the more acidic sulfate ion, the phosphate ion decreases the energy levels of the transition states of the addition of water at the Cbeta of the PLP-alpha-aminocrotonate aldimine and the transaldimination to form L-threonine. Threonine synthase is in the closed form, when the substrate and the intermediates are bound to the enzyme
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-
?
O-phospho-L-homoserine + H2O
L-threonine + phosphate
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
O-phospho-L-homoserine + H2O
L-threonine + phosphate
show the reaction diagram
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-
-
?
O-phospho-L-homoserine + H2O
L-threonine + phosphate
show the reaction diagram
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.61
L-Vinylglycine
pH 8.0, 25°C
0.8
O-phospho-L-homoserine
pH 8.0, 25°C
0.034
phosphate
pH 8.0, 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0059
L-Vinylglycine
pH 8.0, 25°C
5.2
O-phospho-L-homoserine
pH 8.0, 25°C
0.0013
phosphate
pH 8.0, 25°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
P83823_THETH
351
0
37010
TrEMBL
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apo-protein and in complex with 2-amino-5-phosphonopentanoic acid and with (E)-4-(3-hydroxy-2-methyl-5-(phosphonooxymethyl)pyridin-4-yl)-2-oxobut-3-enoic acid. The enzyme does not undergo any global conformational change upon the binding of pyridoxal 5'-phosphate. The binding of the substrate analog 2-amino-5-phosphonopentanoic acid to the holoenzyme induces a large conformational change from the open to the closed form in which the small domain moves as a rigid body to close the active site. This closed structure is maintained in the complex with (E)-4-(3-hydroxy-2-methyl-5-(phosphonooxymethyl)pyridin-4-yl)-2-oxobut-3-enoic acid, indicating that threonine synthase is in the closed form in the enamine and the pyridoxal 5'-phosphate-alpha-aminocrotonate aldimine intermediates
comparative QM/MM calculations. The base that abstracts a proton from the attacking water is the epsilon-amino group of Lys61 rather than the phosphate ion. The phosphate ion is important for stabilizing the transition state of the normal transaldimination to form L-threonine by making a hydrogen bond with the hydroxy group of the L-threonine moiety. Proposal of a mechanism, in which a proton temporarily resides at the phenolate O3' of pyridoxal-5'-phosphate, for the transaldimination process
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hanging drop vapour diffusion method at 293 K, unligated enzyme form and complex with substrate analogue 2-amino-5-phosphonopentanoic acid, structure determined at 2.15 A and 2.0 A resolution
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Omi, R.; Goto, M.; Miyahara, I.; Mizuguchi, H.; Hayashi, H.; Kagamiyama, H.; Hirotsu, K.
Crystal structures of threonine synthase from Thermus thermophilus HB8: conformational change, substrate recognition, and mechanism
J. Biol. Chem.
278
46035-46045
2003
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Manually annotated by BRENDA team
Murakawa, T.; Machida, Y.; Hayashi, H.
Product-assisted catalysis as the basis of the reaction specificity of threonine synthase
J. Biol. Chem.
286
2774-2784
2011
Thermus thermophilus (Q5SL02), Thermus thermophilus HB8 / ATCC 27634 / DSM 579 (Q5SL02)
Manually annotated by BRENDA team
Shoji, M.; Hanaoka, K.; Ujiie, Y.; Tanaka, W.; Kondo, D.; Umeda, H.; Kamoshida, Y.; Kayanuma, M.; Kamiya, K.; Shiraishi, K.; Machida, Y.; Murakawa, T.; Hayashi, H.
A QM/MM study of the L-threonine formation reaction of threonine synthase: implications into the mechanism of the reaction specificity
J. Am. Chem. Soc.
136
4525-4533
2014
Thermus thermophilus
Manually annotated by BRENDA team
Kaur, G.; Subramanian, S.
Evolutionary analysis of a novel zinc ribbon in the N-terminal region of threonine synthase
Cell Cycle
16
1918-1926
2017
Aquifex aeolicus (O66740), Arabidopsis thaliana (Q9S7B5), Brucella melitensis (Q8YFS0), Brucella melitensis 16M (Q8YFS0), Burkholderia thailandensis (Q2SWH9), Burkholderia thailandensis ATCC 700388 (Q2SWH9), Escherichia coli (P00934), Mycobacterium tuberculosis (P9WG59), Mycobacterium tuberculosis H37Rv (P9WG59), Saccharomyces cerevisiae (P16120), Thermus thermophilus (P83823), Thermus thermophilus (Q5SL02)
Manually annotated by BRENDA team