PROSITE documentation PDOC00532

Glycosyl hydrolases family 32 active site





Description

It has been shown [1,2] that the following glycosyl hydrolases can be classified into a single family on the basis of sequence similarities:

  • Inulinase (EC 3.2.1.7) (or inulase) from the fungi Kluyveromyces marxianus.
  • β-fructofuranosidase (EC 3.2.1.26), commonly known as invertase in fungi and plants and as sucrase in bacteria (gene sacA or scrB).
  • Raffinose invertase (EC 3.2.1.26) (gene rafD) from Escherichia coli plasmid pRSD2.
  • Levanase (EC 3.2.1.65) (gene sacC) from Bacillus subtilis.

One of the conserved regions in these enzymes is located in the N-terminal section and contains an aspartic acid residue which has been shown [3], in yeast invertase to be important for the catalytic mechanism. We have used this region as a signature pattern.

Expert(s) to contact by email:

Henrissat B.

Last update:

April 2006 / Pattern revised.

Technical section

PROSITE method (with tools and information) covered by this documentation:

GLYCOSYL_HYDROL_F32, PS00609; Glycosyl hydrolases family 32 active site  (PATTERN)


References

1AuthorsHenrissat B.
TitleA classification of glycosyl hydrolases based on amino acid sequence similarities.
SourceBiochem. J. 280:309-316(1991).
PubMed ID1747104

2AuthorsGunasekaran P., Karunakaran T., Cami B., Mukundan A.G., Preziosi L., Baratti J.
TitleCloning and sequencing of the sacA gene: characterization of a sucrase from Zymomonas mobilis.
SourceJ. Bacteriol. 172:6727-6735(1990).
PubMed ID2254250

3AuthorsReddy V.A., Maley F.
TitleIdentification of an active-site residue in yeast invertase by affinity labeling and site-directed mutagenesis.
SourceJ. Biol. Chem. 265:10817-10820(1990).
PubMed ID2113524



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