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Information on EC 3.2.1.177 - alpha-D-xyloside xylohydrolase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9S7Y7

for references in articles please use BRENDA:EC3.2.1.177
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IUBMB Comments
The enzyme catalyses hydrolysis of a terminal, unsubstituted xyloside at the extreme reducing end of a xylogluco-oligosaccharide. Representative alpha-xylosidases from glycoside hydrolase family 31 utilize a two-step (double-displacement) mechanism involving a covalent glycosyl-enzyme intermediate, and retain the anomeric configuration of the product.
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This record set is specific for:
Arabidopsis thaliana
UNIPROT: Q9S7Y7
Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The taxonomic range for the selected organisms is: Arabidopsis thaliana
Reaction Schemes
Hydrolysis of terminal, non-reducing alpha-D-xylose residues with release of alpha-D-xylose.
Synonyms
alpha-D-xyloside xylohydrolase, alpha-xylosidase, alpha-xylosidase 31A, AtXYL1, AxlA, CjXyl31A, xyl31A, XylS, YicI, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alpha-xylosidase
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AtXYL1
294226
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
alpha-D-xyloside xylohydrolase
The enzyme catalyses hydrolysis of a terminal, unsubstituted xyloside at the extreme reducing end of a xylogluco-oligosaccharide. Representative alpha-xylosidases from glycoside hydrolase family 31 utilize a two-step (double-displacement) mechanism involving a covalent glycosyl-enzyme intermediate, and retain the anomeric configuration of the product.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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the expression level is lower in the apical part of the inflorescence stem when compared with the basal region
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
XYL1_ARATH
915
0
102399
Swiss-Prot
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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contains eight possible glycosylation sites
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
the gene is introduced in a suitable expression vector and used to transform Saccharomyces cerevisiae
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the expression level of AtXYL1 does not show a clear relationship with growth rates
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Iglesias, N.; Abelenda, J.A.; Rodino, M.; Sampedro, J.; Revilla, G.; Zarra, I.
Apoplastic glycosidases active against xyloglucan oligosaccharides of Arabidopsis thaliana
Plant Cell Physiol.
47
55-63
2006
Arabidopsis thaliana, Arabidopsis thaliana (Q9S7Y7)
Manually annotated by BRENDA team
Sampedro, J.; Sieiro, C.; Revilla, G.; Gonzalez-Villa, T.; Zarra, I.
Cloning and expression pattern of a gene encoding an alpha-xylosidase active against xyloglucan oligosaccharides from Arabidopsis
Plant Physiol.
126
910-920
2001
Arabidopsis thaliana (Q9S7Y7), Brassica oleracea var. capitata
Manually annotated by BRENDA team
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