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FEBS Lett. 2013 Mar 18;587(6):799-803. doi: 10.1016/j.febslet.2013.02.004. Epub 2013 Feb 14.

α-Galacturonidase(s): a new class of Family 4 glycoside hydrolases with strict specificity and a unique CHEV active site motif.

Author information

1
Microbial Biochemistry and Genetics Section, Laboratory of Cell and Developmental Biology, NIDCR, National Institutes of Health, Bethesda, MD 20892, USA. jthompson@dir.nidcr.nih.gov

Abstract

The catalytic activity of the Family 4 glycosidase LplD protein, whose active site motif is CHEV, is unknown despite its crystal structure having been determined in 2008. Here we identify that activity as being an α-galacturonidase whose natural substrate is probably α-1,4-di-galacturonate (GalUA2). Phylogenetic analysis shows that LplD belongs to a monophyletic clade of CHEV Family 4 enzymes, of which four other members are also shown to be galacturonidases. Family GH 4 enzymes catalyze the cleavage of the glycosidic bond, via a non-canonical redox-assisted mechanism that contrasts with Koshland's double-displacement mechanism.

PMID:
23416295
PMCID:
PMC3608401
DOI:
10.1016/j.febslet.2013.02.004
[Indexed for MEDLINE]
Free PMC Article

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