Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
1 to 7 of 7  Show
  1. 1
    "Cloning and characterization of two structurally and functionally divergent rhamnogalacturonases from Aspergillus aculeatus."
    Kofod L.V., Kauppinen S., Christgau S., Andersen L.N., Heldt-Hansen H.P., Doerreich K., Dalboege H.
    J. Biol. Chem. 269:29182-29189(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Category: Sequences.
    Strain: KSM 510.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 1 other entry.

  2. 2
    "The backbone of the pectic polysaccharide rhamnogalacturonan I is cleaved by an endohydrolase and an endolyase."
    Azadi P., O'Neill M.A., Bergmann C., Darvill A.G., Albersheim P.
    Glycobiology 5:783-789(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 1 other entry.

  3. 3
    "Rhamnogalacturonase B from Aspergillus aculeatus is a rhamnogalacturonan alpha-L-rhamnopyranosyl-(1-->4)-alpha-D-galactopyranosyluronide lyase."
    Mutter M., Colquhoun I.J., Schols H.A., Beldman G., Voragen A.G.
    Plant Physiol. 110:73-77(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Category: Function.
    Source: UniProtKB/Swiss-Prot (reviewed).
  4. 4
    "Characterization of recombinant rhamnogalacturonan alpha-L-rhamnopyranosyl-(1,4)-alpha-D-galactopyranosyluronide lyase from Aspergillus aculeatus. An enzyme that fragments rhamnogalacturonan I regions of pectin."
    Mutter M., Colquhoun I.J., Beldman G., Schols H.A., Bakx E.J., Voragen A.G.
    Plant Physiol. 117:141-152(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
    Category: Function.
    Source: UniProtKB/Swiss-Prot (reviewed).
  5. 5
    "A stepwise optimization of crystals of rhamnogalacturonan lyase from Aspergillus aculeatus."
    Kadirvelraj R., Harris P., Poulsen J.C., Kauppinen S., Larsen S.
    Acta Crystallogr. D 58:1346-1349(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION.
    Category: Structure.
    Source: UniProtKB/Swiss-Prot (reviewed).
  6. 6
    "Rhamnogalacturonan lyase reveals a unique three-domain modular structure for polysaccharide lyase family 4."
    McDonough M.A., Kadirvelraj R., Harris P., Poulsen J.C., Larsen S.
    FEBS Lett. 565:188-194(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.52 ANGSTROMS) OF 20-527, DISULFIDE BOND.
    Category: PTM / Processing, Structure.
    Source: UniProtKB/Swiss-Prot (reviewed).
  7. 7
    "Structural and biochemical studies elucidate the mechanism of rhamnogalacturonan lyase from Aspergillus aculeatus."
    Jensen M.H., Otten H., Christensen U., Borchert T.V., Christensen L.L., Larsen S., Leggio L.L.
    J. Mol. Biol. 404:100-111(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.52 ANGSTROMS) OF 20-527 OF MUTANTS ALA-169 AND ALA-229, DISULFIDE BOND, FUNCTION.
    Category: Function, Pathology & Biotech, PTM / Processing, Structure.
    Source: UniProtKB/Swiss-Prot (reviewed).
1 to 7 of 7  Show

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health