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Information on EC 4.2.3.1 - threonine synthase and Organism(s) Escherichia coli and UniProt Accession P00934

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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:
Escherichia coli
UNIPROT: P00934
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The taxonomic range for the selected organisms is: Escherichia coli
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
-
-
-
-
threonine synthase
-
-
threonine synthetase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
O-phospho-L-homoserine + H2O = L-threonine + phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
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
-
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
-
-
-
?
DL-3-chloroalanine
pyruvate + NH3 + HCl
show the reaction diagram
-
beta-elimination
-
ir
DL-vinylglycine + H2O
L-threonine
show the reaction diagram
-
-
-
ir
L-allo-threonine + H2O
2-oxobutyrate + NH3
show the reaction diagram
-
beta-elimination
-
ir
L-serine
pyruvate + NH3
show the reaction diagram
-
beta-elimination
-
ir
O-phospho-L-homoserine
?
show the reaction diagram
-
studies on regulatory properties
-
-
?
O-phospho-L-homoserine + H2O
L-threonine + phosphate
show the reaction diagram
threonine
2-oxobutyrate + NH3
show the reaction diagram
-
beta-elimination
-
?
additional information
?
-
-
half-transamination reactions
-
-
?
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
-
-
-
?
O-phospho-L-homoserine
?
show the reaction diagram
-
studies on regulatory properties
-
-
?
O-phospho-L-homoserine + H2O
L-threonine + phosphate
show the reaction diagram
-
threonine synthesis in eukaryotes
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
contains a zinc ribbon domain
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
DL-2-amino-3[(phosphonomethyl)thio]propionic acid
-
Ki: 0.057 mM, kinact: 1.44 min-1
DL-E-2-amino-5-phosphono-4-pentenoic acid
-
Ki: 0.54 mM
L-2,3-methanohomoserine phosphate
-
Ki: 0.01 mM
L-2-amino-3[(phosphonomethyl)thio]propionic acid
L-3-hydroxyhomoserine
-
Ki: 0.05 mM
L-threo-3-hydroxyhomoserine
phosphonovaleric acid
-
Ki: 0.031 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.34
O-phospho-L-homoserine
-
pH 8.0, 25°C
0.5
O-phosphohomoserine
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4
O-phospho-L-homoserine
-
pH 8.0, 25°C
7.33
O-phosphohomoserine
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.057
DL-2-amino-3[(phosphonomethyl)thio]propionic acid
-
kinact: 1.44 min-1
0.54
DL-E-2-amino-5-phosphono-4-pentenoic acid
-
-
0.01
L-2,3-methanohomoserine phosphate
-
-
0.011
L-2-amino-3[(phosphonomethyl)thio]propionic acid
-
-
0.05
L-3-hydroxyhomoserine
-
-
0.006
L-threo-3-hydroxyhomoserine
-
-
0.031
phosphonovaleric acid
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.7
-
purified enzyme from cloned gene
additional information
-
homozygous line from plant 829-2 exhibits 10.1fold and 2.1fold higher activity without and with 0.2 mmol/l S-adenosyl methionine compared to wild type. Homozygous line from plant 829-9 exhibits 25.2fold and 3.8fold higher activity without and with 0.2 mmol/l S-adenosyl methionine compared to wild type. Homozygous line from plant 829-14 exhibits 6.5fold and 1.5fold higher activity without and with 0.2 mmol/l S-adenosyl methionine compared to wild type
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
enzyme assay at
7.8
-
enzyme assay at, recombinant enzyme
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
enzyme assay at, recombinant enzyme
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
suspension culture of Nicotiana tabacum cells expressing E. coli enzyme
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
46000 - 48000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
determination of N-terminal amino acid sequence
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Nicotiana tabacum
-
expression in transgenic Arabidopsis
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
continuous, coupled spectrophotometric threonine synthase assay. The sequential actions of threonine deaminase and hydroxyisocaproate dehydrogenase convert the L-Thr product of TS to alpha-ketobutyrate and then to 2-hydroxybutyrate, respectively, and are monitored as the decrease in absorbance at 340 nm resulting from the concomitant oxidation of beta-nicotinamide adenine dinucleotide to NAD+ by hydroxyisocaproate dehydrogenase
medicine
-
possibly involved in formation of bacteriocidal antimetabolites
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Parsot, C.; Cossart, P.; Saint-Girons, I.; Cohen, G.N.
Nucleotide sequence of thrC and of the transcription termination region of the threonine operon in Escherichia coli K12
Nucleic Acids Res.
11
7331-7345
1983
Escherichia coli
Manually annotated by BRENDA team
Shames, S.L.; Ash, D.E.; Wedler, F.C.; Villafranca, J.J.
Interaction of aspartate and aspartate-derived antimetabolites with the enzymes of the threonine biosynthetic pathway of Escherichia coli
J. Biol. Chem.
259
15331-15339
1984
Escherichia coli
Manually annotated by BRENDA team
Farrington, G.K.; Kumar, A.; Shames, S.L.; Ewaskiewicz, J.I.; Ash, D.A.; Wedler, F.C.
Threonine synthase of Escherichia coli: inhibition by classical and slow-binding analogues of homoserine phosphate
Arch. Biochem. Biophys.
307
165-174
1993
Escherichia coli
Manually annotated by BRENDA team
Laber, B.; Gerbling, K.P.; Harde, C.; Neff, K.H.; Nordhoff, E.; Pohlenz, H.D.
Mechanisms of interaction of Escherichia coli threonine synthase with substrates and inhibitors
Biochemistry
33
3413-3423
1994
Escherichia coli
Manually annotated by BRENDA team
Muhitch, M.J.
Effects of expressing E. coli threonine synthase in tobacco (Nicotiana tabacum L.) suspension culture cells on free amino acid levels, aspartate pathway enzyme activities and uptake of aspartate into the cells
Plant Physiol.
150
16-22
1997
Escherichia coli
-
Manually annotated by BRENDA team
Lee, M.; Martin, M.N.; Hudson, A.O.; Lee, J.; Muhitch, M.J.; Leustek, T.
Methionine and threonine synthesis are limited by homoserine availability and not the activity of homoserine kinase in Arabidopsis thaliana
Plant J.
41
685-696
2005
Escherichia coli
Manually annotated by BRENDA team
Morneau, D.J.; Abouassaf, E.; Skanes, J.E.; Aitken, S.M.
Development of a continuous assay and steady-state characterization of Escherichia coli threonine synthase
Anal. Biochem.
423
78-85
2012
Escherichia coli
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