Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.7.4.16 - thiamine-phosphate kinase and Organism(s) Pyrobaculum calidifontis and UniProt Accession A3MTW6

for references in articles please use BRENDA:EC2.7.4.16
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Pyrobaculum calidifontis
UNIPROT: A3MTW6 not found.
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Pyrobaculum calidifontis
The enzyme appears in selected viruses and cellular organisms
Synonyms
thiamin pyrophosphokinase, thiamine monophosphate kinase, thiamin phosphate kinase, thiamin-monophosphate kinase, thiamine-phosphate kinase, thiamin monophosphate kinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
thiamin phosphate kinase
-
thiamin pyrophosphokinase
-
ATP:thiamin-phosphate phosphotransferase
-
-
-
-
kinase, thiamin monophosphate (phosphorylating)
-
-
-
-
thiamin monophosphatase
-
-
-
-
thiamin monophosphate kinase
-
-
-
-
thiamin monophosphokinase
-
-
-
-
thiamin phosphate kinase
-
-
-
-
thiamin-monophosphate kinase
-
-
-
-
thiamin-phosphate kinase
-
-
-
-
thiamine monophosphate kinase
-
-
-
-
thiamine monophosphokinase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
ATP:thiamine-phosphate phosphotransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9068-23-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + thiamine phosphate
ADP + thiamine diphosphate
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
ATP + thiamine phosphate
ADP + thiamine diphosphate
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
AMP
the mode of AMP inhibition is uncompetitive for both thiamine phosphate and ATP
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00013 - 0.28
ATP
0.000043 - 0.0013
thiamine phosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.006 - 0.092
thiamine phosphate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.33 - 46
ATP
68 - 320
thiamine phosphate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.53 - 0.56
AMP
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80 - 120
10% of maximal activity at 80°C, 50% at 100°C, maximal activity at 120°C, inactive on ice
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene Pcal_0657 or THI80
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
biosynthesis pathways of thiamine, thiamine phosphate, and thiamine diphosphate, overview
physiological function
in this archaeon, the phosphorylation of thiamine phosphate is the only way to synthesize thiamine diphosphate, it cannot use exogenous thiamine and direct diphosphorylation for the salvage synthesis of thiamine diphosphate
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
SDS-PAGE and gel filtration, neither R136 nor S196 are important for enzyme dimerization
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R136M
site-directed mutagenesis, the mutant shows 80% reduced activity compared to the wild-type
S196A
site-directed mutagenesis, the mutant shows 90% reduced activity compared to the wild-type
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
purified recombinant ThiL protein, loss of about 45% activity after 15 min at 100°C and 20% after 60 min, ATP can partially stabilize the activity, addition of 0.5 M NaCl or 0.5 M KCl to the enzyme solution does not improve the thermostability
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
ATP stabilizes the enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by metal affinity chromatography and ultrafiltration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene THI80 or Pcal_0657, sequence comparisons, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hayashi, M.; Nosaka, K.
Characterization of thiamin phosphate kinase in the hyperthermophilic archaeon Pyrobaculum calidifontis
J. Nutr. Sci. Vitaminol.
61
369-374
2015
Pyrobaculum calidifontis (A3MTW6), Pyrobaculum calidifontis, Pyrobaculum calidifontis JCM 11548 (A3MTW6)
Manually annotated by BRENDA team