Information on EC 2.7.1.144 - tagatose-6-phosphate kinase

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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
2.7.1.144
-
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RECOMMENDED NAME
GeneOntology No.
tagatose-6-phosphate kinase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + D-tagatose 6-phosphate = ADP + D-tagatose 1,6-bisphosphate
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
D-galactosamine and N-acetyl-D-galactosamine degradation
-
-
galactitol degradation
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lactose and galactose degradation I
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N-acetyl-D-galactosamine degradation
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degradation of sugar alcohols
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metabolism of disaccharids
-
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Galactose metabolism
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Metabolic pathways
-
-
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SYSTEMATIC NAME
IUBMB Comments
ATP:D-tagatose-6-phosphate 1-phosphotransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
39434-00-9
-
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
subsp. lactis MG1820
-
-
Manually annotated by BRENDA team
no activity in Lactobacillus plantarum
-
-
-
Manually annotated by BRENDA team
no activity in Streptococcus faecalis
-
-
-
Manually annotated by BRENDA team
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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-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
-
-
-
-
?
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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 + D-tagatose 6-phosphate
ADP + D-tagatose 1,6-bisphosphate
show the reaction diagram
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
phosphate
-
at high concentrations
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NH4+
-
33.3 mM activates
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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
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.02
-
strain AHT grown on glucose
0.03
-
strain B13 grown on lactose
0.043
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strain Ingbritt grown on glucose
0.045
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strain FA1 grown on glucose
0.05
-
strain OMZ65 grown on lactose
0.144
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grown on galactose
0.158
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strain Ingbritt grown on galactose
0.177
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strain AHT grown on galactose
0.212
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grown on galactose
0.24
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strain Ingbritt grown on lactose
0.247
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strain FA1 grown on lactose
0.303
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grown on galactose
0.374
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strain AHT grown on lactose
0.477
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strain FA1 grown on galactose
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
in potassium phosphate buffer
8
-
in Hepes buffer
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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
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Enterococcus faecalis (strain ATCC 700802 / V583)
Enterococcus faecalis (strain ATCC 700802 / V583)
Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262)
Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262)
Rhizobium meliloti (strain 1021)
Staphylococcus aureus (strain COL)
Staphylococcus aureus (strain NCTC 8325)
Staphylococcus aureus (strain NCTC 8325)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
52000
-
alpha2, 2 * 52000, SDS-PAGE
82000
-
gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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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
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanol stabilizes during purification
-
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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
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native and mutant protein from Escherichia coli
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli; native enzyme and L124M, L125M double mutant expressed in Escherichia coli BL21(DE3)
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ENGINEERING
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
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LINKS TO OTHER DATABASES (specific for EC-Number 2.7.1.144)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)