Information on EC 2.7.1.50 - hydroxyethylthiazole kinase

New: Word Map on EC 2.7.1.50
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Search Reference ID:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY hide
2.7.1.50
-
RECOMMENDED NAME
GeneOntology No.
hydroxyethylthiazole kinase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Metabolic pathways
-
-
thiamine formation from pyrithiamine and oxythiamine (yeast)
-
-
Thiamine metabolism
-
-
thiamine salvage II
-
-
thiamine salvage IV (yeast)
-
-
vitamin B1 metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:4-methyl-5-(2-hydroxyethyl)thiazole 2-phosphotransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9026-56-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
bv. viciae strain 3841
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
THI6 is a bifunctional enzyme of the thiamin biosynthetic pathway
physiological function
the N-terminal domain of THI6 catalyzes the ligation of the thiamin thiazole and pyrimidine moieties to form thiamin phosphate, and the C-terminal domain catalyzes the phosphorylation of 4-methyl-5-hydroxyethylthiazole in a salvage pathway
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP + 4-methyl-5-(2-hydroxyethyl)thiazole
AMP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
show the reaction diagram
-
3.4% of the activity with ATP
-
-
?
ATP + 4-methyl-5-(2-hydroxyethyl)thiazole
ADP + 4-methyl-5-(2-phosphoethyl)thiazole
show the reaction diagram
-
-
-
-
?
ATP + 4-methyl-5-(2-hydroxyethyl)thiazole
ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
show the reaction diagram
CTP + 4-methyl-5-(2-hydroxyethyl)thiazole
CDP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
show the reaction diagram
-
13.7% of the activity with ATP
-
-
?
dATP + 4-methyl-5-(2-hydroxyethyl)thiazole
dADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
show the reaction diagram
-
24.8% of the activity with ATP
-
-
?
GTP + 4-methyl-5-(2-hydroxyethyl)thiazole
GDP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
show the reaction diagram
-
3.2% of the activity with ATP
-
-
?
UTP + 4-methyl-5-(2-hydroxyethyl)thiazole
UDP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
show the reaction diagram
-
75.1% of the activity with ATP
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + 4-methyl-5-(2-hydroxyethyl)thiazole
ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
10 mM, stimulates as effectively as Mg2+
Mn2+
-
stimulates, 42.7% as effectively as Mg2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-Aminohydroxyethylthiazole
-
-
PCMB
-
0.01 mM, 98.5% inhibition, inhibition prevented by addition of 2-mercaptoethanol
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.79
ATP
-
pH 7.5, 37C
0.0057
hydroxyethylthiazole
-
pH 7.5, 37C
additional information
additional information
-
modeling of stationary points along the reaction pathway, determination of relative energies of the transition state and product
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0021
2-Aminohydroxyethylthiazole
-
pH 7.5, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4 - 9.2
-
pH 7.4: about 80% of activity maximum, pH 9.2: about 25% of activity maximum
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Staphylococcus aureus (strain MRSA252)
Staphylococcus aureus (strain MRSA252)
Staphylococcus aureus (strain MRSA252)
Staphylococcus aureus (strain MRSA252)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
470000
-
bifunctional enzyme with hydroxyethylthiazole kinase and thiamine-phosphate pyrophosphorylase activity, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homohexamer
the six protomers form a cage-like structure. Each protomer is composed of two domains, which are structurally homologous to their monofunctional bacterial counterparts. Two loop regions not found in the bacterial enzymes provide interactions between the two domains
homotrimer
3 * 28950 Da, crystal structure, calculated
octamer
-
8 * 60000, bifunctional enzyme with hydroxyethylthiazole kinase and thiamine-phosphate pyrophosphorylase activity, SDS-PAGE
trimer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystallization by vapor diffusion equilibration, crystal structure at 1.5 A resolution
-
purified recombinant detagged enzyme, in complex with beta,gamma-methyleneadenosine 5'-diphosphate, thiamin phosphate, 4-amino-5-hydroxymethyl-2-trifluoromethylpyrimidine diphosphate, or 4-methyl-5-hydroxyethylthiazole phosphate, hanging-drop vapor diffusion method, mixing of0.001 ml protein solution with 0.001 ml of reservoir solution containing 0.1 M HEPES, pH 7.5, 0.2-0.25 M MgCl2, and 25-32% PEG400, 22C, 2-3 days, method optimization, X-ray diffraction structure determination and analysis at 2.6-3.3 A resolution, modeling
enzyme with a phosphate ion occupying the position of the beta-phosphate of the nucleotide, mixing of 0.001 ml of protein solution containing 1.95 mg/ml protein in 20 mM Tris-HCl containing 200 mM NaCl and 1 mM DTT, pH 8.0, with 0.001 ml of reservoir solution containing 0.1 M CHESS buffer, pH 9.3, and 0.88 M sodium citrate as the precipitant, 20C, 1 week, 25% v/v glycerol for cryoprotection, X-ray diffraction structure determination and analysis at 1.85 A resolution
-
precipitant: sodium citrate, pH 9.3, 293 K
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80C, about 50% loss of activity after 1 month
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
bifunctional enzyme with hydroxyethylthiazole kinase and thiamine-phosphate pyrophosphorylase activity
-
heat treatment (363 K, 13 min), centrifugation, ion exchange chromatography, hydroxyapatite chromatography, gel filtration,
recombinant enzyme from Escherichia coli strain BL21-CodonPlus(DE3)-RIL by gel filtration, anion exchange chromatography to over 95% purity
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, cleavage of the tag by TEV protease, and another step of nickel affinity chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21-CodonPlus(DE3)-RIL
expression in Escherichia coli strain BL21-CodonPlus(DE3)-RIL
-
expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C198D
-
increase in catalytic activity, catalytic field predictions
Show AA Sequence (4953 entries)
Please use the Sequence Search for a certain query.