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
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
porphyran
sulfate + porphyran containing 3,6-anhydrogalactose residues
show the reaction diagram
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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
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activity is dependent on the presence of a bi- or tervalent cation which is not Mg2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Al3+
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Ca2+
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Cd2+
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Cu2+
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NH4F
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Ni2+
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Borate
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
6.8 - 9.2
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pH 6.8: about 45% of activity maximum, pH 9.2: about 35% of activity maximum
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
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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
partial
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