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Literature summary extracted from

  • Stressler, T.; Reichenberger, K.; Glueck, C.; Leptihn, S.; Pfannstiel, J.; Swietalski, P.; Kuhn, A.; Seitl, I.; Fischer, L.
    A natural variant of arylsulfatase from Kluyveromyces lactis shows no formylglycine modification and has no enzyme activity (2018), Appl. Microbiol. Biotechnol., 102, 2709-2721 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.6.1 expression in Escherichia coli Kluyveromyces lactis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.6.1 p-cresol sulfate + H2O Kluyveromyces lactis
-
p-cresol + sulfate
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.1.6.1 Kluyveromyces lactis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.6.1 recombinant protein Kluyveromyces lactis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.6.1 p-cresol sulfate + H2O
-
Kluyveromyces lactis p-cresol + sulfate
-
?

General Information

EC Number General Information Comment Organism
3.1.6.1 physiological function strain Kluyveromyces lactis DSM 70799 has no arylsulfatase activity, whereas the strain GG799 does. The only difference is a base substitution at position 415 resulting in an amino acid exchange from R139 in strain DSM 70799 to S139 in strain GG799. Amino acid position 139 is far away from the catalytic site of the arylsulfatase. The posttranslational modification of C56 to formylglycine is not found in the R139 variant. By contrast, the C56 residue of the S139 variant is modified. The inactive R139 variant exhibits a different structure regarding folding and packing compared to the active S139 variant Kluyveromyces lactis