The modular xylanase Xyn10A from Rhodothermus marinus is cell-attached, and its C-terminal domain has several putative homologues among cell-attached proteins within the phylum Bacteroidetes

FEMS Microbiology Letters

Volumn 241, Issue 2, 2004, Pages 233-242

  Karlsson, Eva Nordberg ^a   Hachem, Maher Abou ^a   Ramchuran, Santosh ^a   Costa, Hugo ^a   Holst, Olle ^a   Svenningsen, Åsa Fex ^a   Hreggvidsson, Gudmundur O ^b  

^a LUND UNIVERSITY   (Sweden)

^b Prokaria Ltd   (Iceland)

Author keywords

Bacteroidetes; Cell attachment; Xylanase

Indexed keywords

ENZYME ANTIBODY; UNCLASSIFIED DRUG; XYLAN ENDO 1,3 BETA XYLOSIDASE; XYLANASE 10A;

ANTIBODY SPECIFICITY; ARTICLE; BACTERIAL GROWTH; BACTEROIDES; CARBOXY TERMINAL SEQUENCE; CELL ADHESION; CELL SURFACE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ASSAY; IMMUNOCYTOCHEMISTRY; MODULATION; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; RHODOTHERMUS MARINUS; SEQUENCE HOMOLOGY; THEORY;

AMINO ACID SEQUENCE; BACTEROIDETES; CELL WALL; COMPUTATIONAL BIOLOGY; GENE EXPRESSION REGULATION, BACTERIAL; IMMUNOHISTOCHEMISTRY; MOLECULAR SEQUENCE DATA; PHYLOGENY; RHODOTHERMUS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; XYLAN ENDO-1,3-BETA-XYLOSIDASE;

BACTEROIDETES; CYTOPHAGA; CYTOPHAGA HUTCHINSONII; RHODOTHERMUS MARINUS;

EID: 10444265893     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.femsle.2004.10.026     Document Type: Article

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