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Literature summary for 2.8.2.21 extracted from

  • Rüter, E.R.; Kresse, H.
    Partial purification and characterization of 3-phosphoadenylylsulfate:keratan sulfate sulfotransferases (1984), J. Biol. Chem., 259, 11771-11776.
    View publication on PubMed
Search for more literature for 2.8.2.21

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
140000
-
 sulfotransferase II, gel filtration Bos taurus
220000
-
 sulfotransferase I, gel filtration Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
sulfotransferase I and II Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
cornea
-
 Bos taurus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Bos taurus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3'-phosphoadenylylsulfate + agarose sulfotransferase I active, sulfotransferase II not Bos taurus adenosine 3',5'-bisphosphate + ?
-
 ?
3'-phosphoadenylylsulfate + chitin dodecylsaccharide sulfotransferase I and II Bos taurus adenosine 3',5'-bisphosphate + ?
-
 ?
3'-phosphoadenylylsulfate + keratan sulfate both enzyme species react best with keratan sulfate segments exhibiting a relatively high degree of sulfation Bos taurus adenosine 3',5'-bisphosphate + keratan 6'-sulfate specificity, sulfotransferase I: 60% of the sulfate ester groups formed are linked to the C-6 atom of galactosyl residues, the rest to the C-6 atom of N-acetylglucosamine, sulfotransferase II: 23% of the newly formed sulfate ester groups are on galactosyl and 77% on N-acetylglucosaminyl residues ?
3'-phosphoadenylylsulfate + keratan sulfate no activity with keratansulfate-derived oligosaccharides Bos taurus adenosine 3',5'-bisphosphate + keratan 6'-sulfate specificity, sulfotransferase I: 60% of the sulfate ester groups formed are linked to the C-6 atom of galactosyl residues, the rest to the C-6 atom of N-acetylglucosamine, sulfotransferase II: 23% of the newly formed sulfate ester groups are on galactosyl and 77% on N-acetylglucosaminyl residues ?
3'-phosphoadenylylsulfate + keratan sulfate very weak activity towards desulfated keratan sulfate Bos taurus adenosine 3',5'-bisphosphate + keratan 6'-sulfate specificity, sulfotransferase I: 60% of the sulfate ester groups formed are linked to the C-6 atom of galactosyl residues, the rest to the C-6 atom of N-acetylglucosamine, sulfotransferase II: 23% of the newly formed sulfate ester groups are on galactosyl and 77% on N-acetylglucosaminyl residues ?
3'-phosphoadenylylsulfate + keratan sulfate partially desulfated Bos taurus adenosine 3',5'-bisphosphate + keratan 6'-sulfate specificity, sulfotransferase I: 60% of the sulfate ester groups formed are linked to the C-6 atom of galactosyl residues, the rest to the C-6 atom of N-acetylglucosamine, sulfotransferase II: 23% of the newly formed sulfate ester groups are on galactosyl and 77% on N-acetylglucosaminyl residues ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
15
-
-
 Bos taurus

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
15 37 15°C: optimum, 37°C: 10% sulfotransferase I activity and 14% sulfotransferase II activity of maximum Bos taurus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
 sulfotransferase I Bos taurus
8.5
-
 sulfotransferase II Bos taurus