3bsqA Abstract: Difference between revisions

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Sulfatases are hydrolytic enzymes which cleave sulfuric ester bonds of their substrates. Sulfatases show highly conserved sequence features, especially at the N-terminal region where the catalytic site is located. Arylsulfatase K is a water-soluble enzyme found in the endoplasmic retuculum (ER). Sequence alignment studies show that the catalytic site of STS shares many key residues within ASK in addition to the abovementioned universally conserved residues, suggesting that the substrates and function of STS may be similar to that of ASK (Natasha you really need to add something about evolution here).
Sulfatases are hydrolytic enzymes, which cleave sulfuric ester bonds of their substrate. Sulfatases show highly conserved sequence feteures, especially in in the N-terminal region where the catalytic site is found. Arylsulfatase K is a water soluble enzyme found in endoplasmic retuculums (ER) of the cell. Structural studies show highly conserved features in ASK N-terminus with steroid sulfatase (STS) N-terminal catalytic site.

Revision as of 10:44, 7 June 2008

Sulfatases are hydrolytic enzymes which cleave sulfuric ester bonds of their substrates. Sulfatases show highly conserved sequence features, especially at the N-terminal region where the catalytic site is located. Arylsulfatase K is a water-soluble enzyme found in the endoplasmic retuculum (ER). Sequence alignment studies show that the catalytic site of STS shares many key residues within ASK in addition to the abovementioned universally conserved residues, suggesting that the substrates and function of STS may be similar to that of ASK (Natasha you really need to add something about evolution here).