Information on EC 2.5.1.5 - galactose-6-sulfurylase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.5.1.5
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RECOMMENDED NAME
GeneOntology No.
galactose-6-sulfurylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
eliminates sulfate from the D-galactose 6-sulfate residues of porphyran, producing 3,6-anhydrogalactose residues
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
sulfate group removal
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SYSTEMATIC NAME
IUBMB Comments
D-galactose-6-sulfate:alkyltransferase (cyclizing)
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CAS REGISTRY NUMBER
COMMENTARY hide
9030-36-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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mucopolysaccharidose, upon silencing significant increase of sulfated substrates, due to overexpression significant decline of all substrates and up-regulation of chondroitin sulfate-containing proteoglycan (syndecan-1 and decorin) expression, increase of soluble syndecan-1 protein
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
mu-carrageenan
sulfate + kappa-carrageenan
show the reaction diagram
ni-carrageenan
sulfate + iota-carrageenan
show the reaction diagram
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-
?
porphyran
sulfate + agarose
show the reaction diagram
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?
porphyran
sulfate + porphyran containing 3,6-anhydrogalactose residues
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
mu-carrageenan
sulfate + kappa-carrageenan
show the reaction diagram
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-
-
-
?
ni-carrageenan
sulfate + iota-carrageenan
show the reaction diagram
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-
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?
porphyran
sulfate + agarose
show the reaction diagram
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-
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-
?
porphyran
sulfate + porphyran containing 3,6-anhydrogalactose residues
show the reaction diagram
-
eliminates sulfate from the D-galactose 6-sulfate residues of porphyran producing 3,6-anhydrogalactose residues
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Borate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.03782
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crude extract, at pH 7.0 and 40C
0.1865
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after purification, at pH 7.0 and 40C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.6 - 7.8
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sodium tetraborate/HCl buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9.5
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the activity at pH 6.5 and 9.5 is 23.6% and 0.9% of the maximum activity, respectively
6.8 - 9.2
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pH 6.8: about 45% of activity maximum, pH 9.2: about 35% of activity maximum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 60
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enzyme activity gradually increases in the temperature range from 10 to 40C. The enzyme activity is less than half of the highest activity when the temperature is not more than 30C and higher than 60C. The enzyme activity is completely absent at 70C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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; primary mammary epithelial cell, highest activity of galactose-6-sulfatase and arylsulfatase A of the cells tested
Manually annotated by BRENDA team
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; low activity of steroid sulfatase, arylsulfatase B, arylsulfatase A, and galactose-6-sulfatase, but not iduronate-2-sulfatase
Manually annotated by BRENDA team
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; highest activity of steroid sulfatase and arylsulfatase B of the cells tested
Manually annotated by BRENDA team
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; low activity of steroid sulfatase, arylsulfatase B, arylsulfatase A, and galactose-6-sulfatase, but not iduronate-2-sulfatase
Manually annotated by BRENDA team
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 65000, SDS-PAGE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the addition of 5% (w/v) sucrose and trehalose prior to lyophilization can retain nearly 100% enzymatic activity, compared to 19% for the lyophilized control. Polyol sucrose and amino acid glycine enhance the thermal stability of the enzyme, while polyol mannitol decreases the thermal stability
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, lyophilized enzyme, 40 days, no loss of activity
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-20C, with glycerol, 20 days, 20% loss of activity
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4C, crude extract at pH 5.0, 1 day, more than 60% loss of activity
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4C, crude extract at pH 7.0 with 10 mM beta-mercaptoethanol, 7 days, no loss of activity
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4C, crude extract at pH 7.0, 7 days, 45% loss of activity
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4C, gradual loss of activity in solution
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room temperature, stable for at least several months as a freeze-dried powder
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, HiTrap DEAE column chromatography, and phenyl column chromatography
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partial
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