Information on EC 2.7.1.119 - hygromycin-B 7''-O-kinase

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The expected taxonomic range for this enzyme is: Streptomyces hygroscopicus

EC NUMBER
COMMENTARY hide
2.7.1.119
-
RECOMMENDED NAME
GeneOntology No.
hygromycin-B 7''-O-kinase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + hygromycin B = ADP + 7''-O-phosphohygromycin B
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:hygromycin-B 7''-O-phosphotransferase
Phosphorylates the antibiotics hygromycin B, 1-N-hygromycin B and destomycin, but not hygromycin B2, at the 7''-hydroxy group in the destomic acid ring.
CAS REGISTRY NUMBER
COMMENTARY hide
88361-67-5
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + hygromycin B
ADP + 7''-O-phosphohygromycin
show the reaction diagram
ATP + hygromycin B
ADP + 7''-O-phosphohygromycin B
show the reaction diagram
-
-
-
?
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 + hygromycin B
ADP + 7''-O-phosphohygromycin
show the reaction diagram
ATP + hygromycin B
ADP + 7''-O-phosphohygromycin B
show the reaction diagram
P09979
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
hygromycin B
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0364 - 0.0822
ATP
0.00056 - 0.03
hygromycin B
additional information
additional information
-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.5 - 5.6
ATP
6.4 - 8
hygromycin B
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
59.1 - 68.1
ATP
4
267 - 383
hygromycin B
4532
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.61 - 1.27
hygromycin B
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.6 - 8.5
-
pH 6.6: about 40% of maximal activity, pH 8.5: about 65% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41000
-
1 * 41000, SDS-PAGE
42000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 37980, wild-type enzyme, sequence calculation, x * 38348, enzyme mutant HYG10, sequence calculation
monomer
-
1 * 41000, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
T1/2 of wild-type enzyme HYG
48 - 74
T1/2 of mutant enzyme HYG10, Tmax is 74°C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
glycerol and bovine serum albumin stabilize
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, in 50% v/v glycerol and 0.1% bovine serum albumin, stable for up to 6 months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged enzyme fom Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography, and gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene hyg, subcloning in Escherichia coli strain JM109, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3), recombinant enzyme expression from plasmid pT8S-P31 in Thermus thermophilus strain B27 TH104 providing hygromycin B resistance up to 60°C, while recombinant expression of a mutant variant HYG10, containing seven substitutions and a duplication, provides HgB resistance up to 74°C
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L79F/S83L/G189R/E237K/S252P/D285N/L290M
random mutagenesis, mutant HYG10 contains seven substitutions and a duplication, it is thermostabilized compared to the wild-type enzyme, three-dimensional structure analysis, overview. Substitutions G189R, E237K, and D285N are located at the protein surface. The mutant shows altered kinetics at 45°C compared to the wild-type enzyme