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From phosphatases to vanadium peroxidases: a similar architecture of the active site.

ABSTRACT: We show here that the amino acid residues contributing to the active sites of the vanadate containing haloperoxidases are conserved within three families of acid phosphatases; this suggests that the active sites of these enzymes are very similar. This is confirmed by activity measurements showing that apochloroperoxidase exhibits phosphatase activity. These observations not only reveal interesting evolutionary relationships between these groups of enzymes but may also have important implications for the research on acid phosphatases, especially glucose-6-phosphatase-the enzyme affected in von Gierke disease-of which the predicted membrane topology may have to be reconsidered.

SUBMITTER: Hemrika W

PROVIDER: S-EPMC20055 | biostudies-literature | 1997 Mar

REPOSITORIES: biostudies-literature

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From phosphatases to vanadium peroxidases: a similar architecture of the active site.

Hemrika W W Renirie R R Dekker H L HL Barnett P P Wever R R

Proceedings of the National Academy of Sciences of the United States of America 19970301 6

We show here that the amino acid residues contributing to the active sites of the vanadate containing haloperoxidases are conserved within three families of acid phosphatases; this suggests that the active sites of these enzymes are very similar. This is confirmed by activity measurements showing that apochloroperoxidase exhibits phosphatase activity. These observations not only reveal interesting evolutionary relationships between these groups of enzymes but may also have important implications ...[more]

PMID: 9122162

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