Information on EC 2.5.1.5 - galactose-6-sulfurylase

for references in articles please use BRENDA:EC2.5.1.5
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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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?
porphyran
sulfate + agarose
show the reaction diagram
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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 40°C
0.1865
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after purification, at pH 7.0 and 40°C
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 40°C. The enzyme activity is less than half of the highest activity when the temperature is not more than 30°C and higher than 60°C. The enzyme activity is completely absent at 70°C
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65000
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1 * 65000, SDS-PAGE
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
-20°C, lyophilized enzyme, 40 days, no loss of activity
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-20°C, with glycerol, 20 days, 20% loss of activity
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4°C, crude extract at pH 5.0, 1 day, more than 60% loss of activity
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4°C, crude extract at pH 7.0 with 10 mM beta-mercaptoethanol, 7 days, no loss of activity
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4°C, crude extract at pH 7.0, 7 days, 45% loss of activity
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4°C, 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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