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Information on EC 2.7.1.144 - tagatose-6-phosphate kinase and Organism(s) Staphylococcus aureus and UniProt Accession P0A0B9

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Staphylococcus aureus
UNIPROT: P0A0B9 not found.
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The taxonomic range for the selected organisms is: Staphylococcus aureus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
tagatose-6-phosphate kinase, d-tagatose-6-phosphate kinase, phosphotagatokinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D-tagatose-6-phosphate kinase
-
phosphotagatokinase
-
D-tagatose 6-phosphate kinase
-
-
-
-
tagatose 6-phosphate kinase (phosphorylating)
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + D-tagatose 6-phosphate = ADP + D-tagatose 1,6-bisphosphate
show the reaction diagram
mechanism suggested
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
ATP:D-tagatose-6-phosphate 1-phosphotransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
39434-00-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + D-tagatose 6-phosphate
ADP + D-tagatose 1,6-bisphosphate
show the reaction diagram
second step of the D-tagatose-6-phosphate pathway which is the direct catabolic pathway for lactose
-
-
?
ATP + D-fructose 6-phosphate
ADP + D-fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
-
?
ATP + D-tagatose 6-phosphate
ADP + D-tagatose 1,6-bisphosphate
show the reaction diagram
CTP + D-tagatose 6-phosphate
CDP + D-tagatose 1,6-bisphosphate
show the reaction diagram
-
-
-
-
?
GTP + D-tagatose 6-phosphate
GDP + D-tagatose 1,6-bisphosphate
show the reaction diagram
-
-
-
-
?
ITP + D-tagatose 6-phosphate
IDP + D-tagatose 1,6-bisphosphate
show the reaction diagram
-
-
-
-
?
TTP + D-tagatose 6-phosphate
TDP + D-tagatose 1,6-bisphosphate
show the reaction diagram
-
-
-
-
?
UTP + D-tagatose 6-phosphate
UDP + D-tagatose 1,6-bisphosphate
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 + D-tagatose 6-phosphate
ADP + D-tagatose 1,6-bisphosphate
show the reaction diagram
second step of the D-tagatose-6-phosphate pathway which is the direct catabolic pathway for lactose
-
-
?
ATP + D-tagatose 6-phosphate
ADP + D-tagatose 1,6-bisphosphate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
required, two ions bound to the active site when substrate and cofactor are bound
Cd2+
-
8% of the activation with Mg2+, at 1.3 mM
Co2+
-
54% of the activation with Mg2+, at 1.3 mM
K+
-
33.3 mM activates
Mg2+
-
absolute requirement for a divalent cation, a Mg2+ : ATP ratio of 2.0-2.5 is required for maximal activity
Mn2+
-
27% of the activation with Mg2+, at 1.3 mM
Ni2+
-
15% of the activation with Mg2+, at 1.3 mM
Rb+
-
33.3 mM activates
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
phosphate
-
at high concentrations
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NH4+
-
33.3 mM activates
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.16
ATP
0.15
D-fructose 6-phosphate
0.016
D-tagatose 6-phosphate
0.4
GTP
0.17
ITP
0.9
UTP
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.144
-
grown on galactose
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
in potassium phosphate buffer
8
-
in Hepes buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 9.5
-
pH 7.5: about 75% of maximal activity, pH 9.5: about 55% of maximal activity, glycylglycine buffer
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
52000
-
alpha2, 2 * 52000, SDS-PAGE
82000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
gel filtration data, crystal structure analysis, two monomers associate via interactions between their lid domains, which come together to form a beta-barrel structure known as a beta-clasp
dimer
-
alpha2, 2 * 52000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
high resolution structures of D-tagatose-6-phosphate kinase (LacC) in two crystal forms. The structures define LacC in apoform, in binary complexes with ADP or the cofactor analogue adenosine 5'-(beta,gamma-imino)triphosphate, and in a ternary complex with adenosine 5'-(beta,gamma-imino)triphosphate and D-tagatose-6-phosphate. LacC adopts a closed structure required for phosphoryl transfer only when both substrate and co-factor are bound
native and L124M, L125M double mutant crystallized by hanging drop vapor diffusion method in apoform, in binary complexes with ADP or the cofactor analogue AMP-PNP, and in a ternary complex with AMP-PNP and D-tagatose-6-phosphate, wild-type protein give crystals that diffracte only to low resolution, the SeMet double mutant protein produced much more ordered crystals
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L124M/L125M
wild-type protein give crystals that diffracte only to low resolution, the SeMet double mutant protein produced much more ordered crystals
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanol stabilizes during purification
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 20 mM potassium phosphate buffer, pH 7.5, 20% v/v glycerol, 0.2% v/v 2-mercaptoethanol, stable for several months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native and mutant protein from Escherichia coli
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
native enzyme and L124M, L125M double mutant expressed in Escherichia coli BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Anderson, R.L.; Bissett, D.L.
D-Tagatose-6-phosphate kinase from Staphylococcus aureus
Methods Enzymol.
90
87-91
1982
Staphylococcus aureus
-
Manually annotated by BRENDA team
Bissett, D.L.; Anderson, R.L.
Lactose and D-galactose metabolism in Staphylococcus aureus. III: Purification and properties of D-tagatose-6-phosphate kinase
J. Biol. Chem.
255
8745-8749
1980
Staphylococcus aureus
Manually annotated by BRENDA team
Schleifer, K.H.; Hartinger, A.; Gtz, F.
Occurence of D-tagatose-6-phosphate pathway of D-galactose metabolism among Staphylococci
FEMS Microbiol. Lett.
3
9-11
1978
Staphylococcus aureus, no activity in Lactobacillus plantarum, no activity in Streptococcus faecalis, Staphylococcus epidermidis, Staphylococcus hominis
-
Manually annotated by BRENDA team
Miallau, L.; Hunter, W.N.; McSweeney, S.M.; Leonard, G.A.
Structures of Staphylococcus aureus D-tagatose-6-phosphate kinase implicate domain motions in specificity and mechanism
J. Biol. Chem.
282
19948-19957
2007
Staphylococcus aureus (P0A0B9), Staphylococcus aureus
Manually annotated by BRENDA team