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Information on EC 4.2.3.1 - threonine synthase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9S7B5
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4.2.3.1 threonine synthaseIUBMB Comments
A pyridoxal-phosphate protein.
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Word Map
- 4.2.3.1
- cystathionine
-
gamma-synthase
- o-phosphohomoserine
-
plp-dependent
-
aspartate-derived
-
rhizocticins
- lactofermentum
-
aldimine
- agriculture
- medicine
- nutrition
- analysis
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
threonine synthase, threonine synthetase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
synthase, threonine
-
-
-
-
threonine synthetase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
O-phospho-L-homoserine + H2O = L-threonine + phosphate
reaction proceeds via phosphate removal and isomerization from primary to secondary alcohol
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-
SYSTEMATIC NAME
IUBMB Comments
O-phospho-L-homoserine phosphate-lyase (adding water; L-threonine-forming)
A pyridoxal-phosphate protein.
CAS REGISTRY NUMBER
COMMENTARY
9023-97-6
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
O-phospho-L-homoserine + H2O
L-threonine + phosphate
-
-
?
O-phospho-L-homoserine + H2O
L-threonine + phosphate
last reaction in the synthesis of threonine from aspartate
-
?
O-phospho-L-homoserine + H2O
L-threonine + phosphate
threonine synthesis in eukaryotes
-
-
?
O-phospho-L-homoserine + H2O
L-threonine + phosphate
-
enzyme at the metabolic branch point between methionine and threonine biosynthesis
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
O-phospho-L-homoserine + H2O
L-threonine + phosphate
-
enzyme at the metabolic branch point between methionine and threonine biosynthesis
-
?
O-phospho-L-homoserine + H2O
L-threonine + phosphate
last reaction in the synthesis of threonine from aspartate
-
?
O-phospho-L-homoserine + H2O
L-threonine + phosphate
threonine synthesis in eukaryotes
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
S-adenosylmethionine
-
affects both Km and Vmax by allosteric and cooperative transition of enzyme, two mol per mol enzyme, 25fold decrease of Km at 0.06 mM
S-adenosylmethionine
-
3-20fold increase of specific activity in various recombinant enzymes at 0.2 mM
S-adenosylmethionine
-
same binding site as inhibitor AMP, 85fold increase of activity, maximum activity at 0.06-0.25 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). THRC1_ARATH
526
0
57777
Swiss-Prot
Chloroplast (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
58000
-
2 * 58000, comparison of nucleotide sequence and molecular mass of native enzyme
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
four-domain dimer with a two-stranded beta-sheet arm protruding from one monomer onto the other
dimer
dimer
-
2 * 58000, comparison of nucleotide sequence and molecular mass of native enzyme
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallographic structure of Arabidopsis thaliana threonine synthase in complex with pyridoxal phosphate and with pyridoxal phosphate and S-adenosylmethionine
hanging-drop vapour-diffusion method, crystal structure of apo threonine synthase as solved at 2.25 A resolution from triclinic crystals
hanging-drop vapour-diffusion method at 293 K. Selenomethionine-substituted apo threonine synthase, 14 Met residues in 58000 Da
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
as one of the few enzymes that are cross-activated by the product of another pathway, S-adenosyl-L-methionine, it has a potential application as a target for herbicides
nutrition
-
interesting with respect to attempts to obtain transgenic plants with elevated levels of essential amino acids Met, Lys, Thr
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Curien, G.; Dumas, R.; Ravanel, S.; Douce, R.
Characterization of an Arabidopsis thaliana cDNA encoding an S-adenosylmethionine-sensitive threonine synthase. Threonine synthase from higher plants
FEBS Lett.
390
85-90
1996
Arabidopsis thaliana
Laber, B.; Maurer, W.; Hanke, C.; Graefe, S.; Ehlert, S.; Messerschmidt, A.; Clausen, T.
Characterization of recombinant Arabidopsis thaliana threonine synthase
Eur. J. Biochem.
263
212-221
1999
Arabidopsis thaliana
Curien, G.; Job, D.; Douce, R.; Dumas, R.
Allosteric activation of Arabidopsis threonine synthase by S-adenosylmethionine
Biochemistry
37
13212-13221
1998
Arabidopsis thaliana
Thomazeau, K.; Curien, G.; Thompson, A.; Dumas, R.; Biou, V.
MAD on threonine synthase: the phasing power of oxidized selenomethionine
Acta Crystallogr. Sect. D
57
1337-1340
2001
Arabidopsis thaliana
Curien, G.; Ravanel, S.; Dumas, R.
A kinetic model of the branch-point between the methionine and threonine biosynthesis pathways in Arabidopsis thaliana
Eur. J. Biochem.
270
4615-4627
2003
Arabidopsis thaliana
Thomazeau, K.; Curien, G.; Dumas, R.; Biou, V.
Crystal structure of threonine synthase from Arabidopsis thaliana
Protein Sci.
10
638-648
2001
Arabidopsis thaliana (Q9S7B5), Arabidopsis thaliana
Mas-Droux, C.; Biou, V.; Dumas, R.
Allosteric threonine synthase. Reorganization of the pyridoxal phosphate site upon asymmetric activation through S-adenosylmethionine binding to a novel site
J. Biol. Chem.
281
5188-5196
2006
Arabidopsis thaliana (Q9S7B5), Arabidopsis thaliana
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)
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