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Titolo:
Pectin degrading glycoside hydrolases of family 28: sequence-structural features, specificities and evolution
Autore:
Markovic, O; Janecek, S;
Indirizzi:
Slovak Acad Sci, Inst Chem, SK-84238 Bratislava, Slovakia Slovak Acad SciBratislava Slovakia SK-84238 -84238 Bratislava, Slovakia Slovak Acad Sci, Inst Mol Biol, SK-84251 Bratislava, Slovakia Slovak Acad Sci Bratislava Slovakia SK-84251 -84251 Bratislava, Slovakia
Titolo Testata:
PROTEIN ENGINEERING
fascicolo: 9, volume: 14, anno: 2001,
pagine: 615 - 631
SICI:
0269-2139(200109)14:9<615:PDGHOF>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
SITE-DIRECTED MUTAGENESIS; PARALLEL BETA-HELIX; NIGER ENDOPOLYGALACTURONASE-II; HYDROPHOBIC CLUSTER-ANALYSIS; ASPERGILLUS-NIGER; POLYGALACTURONASE GENE; ERWINIA-CAROTOVORA; CRYSTAL-STRUCTURE; ACTIVE-SITE; ENCODING POLYGALACTURONASE;
Keywords:
evolution; polygalacturonase; rhamnogalacturonase; xylogalacturonan hydrolase;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
57
Recensione:
Indirizzi per estratti:
Indirizzo: Janecek, S Slovak Acad Sci, Inst Chem, Dubravska Cesta 9, SK-84238 Bratislava, Slovakia Slovak Acad Sci Dubravska Cesta 9 Bratislava Slovakia SK-84238
Citazione:
O. Markovic e S. Janecek, "Pectin degrading glycoside hydrolases of family 28: sequence-structural features, specificities and evolution", PROTEIN ENG, 14(9), 2001, pp. 615-631

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 andthe evolutionary relationships within the entire family 28. The disulfidescommon for the individual enzyme groups were also proposed. With regard tofunctionally 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 fungalexopolygalacturonases and the rhamnogalacturonases form their own cluster on the adjacent branch.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/01/20 alle ore 16:14:55