title: Pectin degrading glycoside hydrolases of family 28: sequence-structural features, specificities and evolution.
abstract: Family 28 belongs to the largest families of glycoside hydrolases. It covers several enzyme specificities of bacterial, fungal, plant and insect origins. This study deals with all available amino acid sequences of family 28 members. First, it focuses on the detailed analysis of 115 sequences of polygalacturonases yielding their evolutionary tree. The large data set allowed modification of some of the existing family 28 sequence characteristics and to draw the sequence features specific for bacterial and fungal exopolygalacturonases discriminating them from the endopolygalacturonases. The evolutionary tree reflects both the taxonomy and specificity so that bacterial, fungal and plant enzymes form their own clusters, the endo- and exo-mode of action being respected, too. The only insect (animal) representative is most related to fungal endopolygalacturonases. The present study brings further: (i) the analysis of available rhamnogalacturonase sequences; (ii) the elucidation of relatedness between the recently added member, the endo-xylogalacturonan hydrolase and the rest of the family; and (iii) revealing the sequence features characteristic of the individual enzyme specificities and the evolutionary relationships within the entire family 28. The disulfides common for the individual enzyme groups were also proposed. With regard to functionally important residues of polygalacturonases, xylogalacturonan hydrolase possesses all of them, while the rhamnogalacturonases, known to lack the histidine residue (His223; Aspergillus niger polygalacturonase II numbering), have a further tyrosine (Tyr291) replaced by a conserved tryptophan. Evolutionarily, the xylogalacturonan hydrolase is most related to fungal exopolygalacturonases and the rhamnogalacturonases form their own cluster on the adjacent branch.
authors.affiliation: Institute of Chemistry, Slovak Academy of Sciences, Dúbravská cesta 9, SK-84238 Bratislava, Slovakia.
authors.forename: O
authors.initials: O
authors.lastname: Markovic
authors.forename: S
authors.initials: S
authors.lastname: Janecek
mesh_terms: D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D000818:Animals; D001419:Bacteria / Q000201:enzymology / Q000235:genetics; D001665:Binding Sites; D017124:Conserved Sequence; D019143:Evolution, Molecular; D005658:Fungi / Q000201:enzymology / Q000235:genetics; D006026:Glycoside Hydrolases / Q000737:chemistry* / Q000145:classification / Q000235:genetics* / Q000378:metabolism; D007313:Insecta / Q000201:enzymology / Q000235:genetics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010368:Pectins / Q000378:metabolism*; D010802:Phylogeny; D010944:Plants / Q000201:enzymology / Q000235:genetics; D011096:Polygalacturonase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D011487:Protein Conformation; D016415:Sequence Alignment; D013045:Species Specificity; D013379:Substrate Specificity
chemical_list: D010368:Pectins; D006026:Glycoside Hydrolases; D011096:Polygalacturonase; C020136:exopolygalacturonase