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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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EC Tree 2 Transferases
2.5 Transferring alkyl or aryl groups, other than methyl groups
2.5.1 Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)
2.5.1.5 galactose-6-sulfurylase
The enzyme appears in viruses and cellular organisms
Reaction Schemes
showeliminates sulfate from the D-galactose 6-sulfate residues of porphyran, producing 3,6-anhydrogalactose residues
Synonyms
gal-6-sulfurylase, d-galactose-6-sulfurylase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D-galactose-6-sulfurylase
galactose 6-sulfatase
-
-
-
-
galactose 6-sulfurylase
-
-
-
-
galactose-6-sulfatase
porphyran sulfatase
-
-
-
-
sulfatase, porphyran
-
-
-
-
galactose-6-sulfatase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
eliminates sulfate from the D-galactose 6-sulfate residues of porphyran, producing 3,6-anhydrogalactose residues
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
sulfate group removal
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-
-
-
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SYSTEMATIC NAME
IUBMB Comments
D-galactose-6-sulfate:alkyltransferase (cyclizing)
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CAS REGISTRY NUMBER
COMMENTARY
9030-36-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
mu-carrageenan
sulfate + kappa-carrageenan
-
Substrates: -
Products: -
Products: -
?
mu-carrageenan
sulfate + kappa-carrageenan
-
Substrates: -
Products: -
Products: -
?
porphyran
sulfate + porphyran containing 3,6-anhydrogalactose residues
-
Substrates: -
Products: -
Products: -
?
porphyran
sulfate + porphyran containing 3,6-anhydrogalactose residues
-
Substrates: eliminates sulfate from the D-galactose 6-sulfate residues of porphyran producing 3,6-anhydrogalactose residues
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
mu-carrageenan
sulfate + kappa-carrageenan
-
Substrates: -
Products: -
Products: -
?
porphyran
sulfate + porphyran containing 3,6-anhydrogalactose residues
-
Substrates: eliminates sulfate from the D-galactose 6-sulfate residues of porphyran producing 3,6-anhydrogalactose residues
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
activity is dependent on the presence of a bi- or tervalent cation which is not Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 9.5
-
the activity at pH 6.5 and 9.5 is 23.6% and 0.9% of the maximum activity, respectively
6.8 - 9.2
-
pH 6.8: about 45% of activity maximum, pH 9.2: about 35% of activity maximum
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 60
-
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
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
SYII.1 is overexpressed in both infertile thalli and thalli within early-stage cystocarp development and regardless of S-source. SYII.1 gene expression is higher than that for SYII.2
brenda
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primary mammary epithelial cell, highest activity of galactose-6-sulfatase and arylsulfatase A of the cells tested
brenda
-
low activity of steroid sulfatase, arylsulfatase B, arylsulfatase A, and galactose-6-sulfatase, but not iduronate-2-sulfatase
brenda
-
highest activity of steroid sulfatase and arylsulfatase B of the cells tested
brenda
-
low activity of steroid sulfatase, arylsulfatase B, arylsulfatase A, and galactose-6-sulfatase, but not iduronate-2-sulfatase
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
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
physiological function
physiological function
-
the enzyme catalyses the conversion of mü-carrageenan into kappa-carrageenan
physiological function
-
galactose-6-sulfurylase is responsible for the removal of sulfate groups to the galactans backbone
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
4°C, crude extract at pH 7.0 with 10 mM beta-mercaptoethanol, 7 days, no loss of activity
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, HiTrap DEAE column chromatography, and phenyl column chromatography
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
methionine and MgSO4 do not affect the transcript number of carbohydrate sulfotransferase and galactose-6-sulfurylase
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SYI.1 expression is higher in early-stage cystocarp development than those in infertile thalli in the presence of both exogenous methionine and MgSO4
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rees, D.A.
Enzymatic desulphation of porphyran
Biochem. J.
80
449-453
1961
Porphyra sp.
brenda
Rees, D.A.
Enzymic synthesis of 3:6-anhydro-L-galactose within porphyran from L-galactose 6-sulphate units
Biochem. J.
81
347-352
1961
Porphyra sp.
brenda
Bhattacharyya, S.; Tobacman, J.K.
Steroid sulfatase, arylsulfatases A and B, galactose-6-sulfatase, and iduronate sulfatase in mammary cells and effects of sulfated and non-sulfated estrogens on sulfatase activity
J. Steroid Biochem. Mol. Biol.
103
20-34
2007
Homo sapiens
brenda
Wang, A.; Islam, M.N.; Qin, X.; Wang, H.; Peng, Y.; Ma, C.
Purification, identification, and characterization of D-galactose-6-sulfurylase from marine algae (Betaphycus gelatinus)
Carbohydr. Res.
388
94-99
2014
Betaphycus gelatinus
brenda
Qin, X.; Ma, C.; Lou, Z.; Wang, H.
Effects of additives on the lyophilized and thermal stability of D-galactose-6-sulfurylase activity from Eucheuma striatum (Rhodophyta)
J. Appl. Phycol.
27
1709-1715
2015
Kappaphycus striatus
-
brenda
del Rosario-Santana, D.; Robaina, R.; Garcia-Jimenez, P.
Jasmonates disrupt carrageenan synthesis during carposporogenesis in the red seaweed Grateloupia imbricata
Front. Mar. Sci.
10
1188493
2023
Grateloupia imbricata
-
brenda
Garcia-Jimenez, P.; Mantesa, S.R.; Robaina, R.R.
Expression of genes related to carrageenan synthesis during carposporogenesis of the red seaweed Grateloupia imbricata
Mar. Drugs
18
432
2020
Grateloupia imbricata
brenda
Del Rosario-Santana, D.; Robaina, R.R.; Garcia-Jimenez, P.
S-Assimilation influences in carrageenan biosynthesis genes during ethylene-induced carposporogenesis in red seaweed Grateloupia imbricata
Mar. Drugs
20
436
2022
Grateloupia imbricata
brenda
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