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Literature summary for 3.2.1.15 extracted from

  • Massa, C.; Guarnaccia, C.; Lamba, D.; Anselmi, C.
    Insight into the structure of an endopolygalacturonase from the phytopathogen Burkholderia cepacia: a biochemical and computational study (2010), Biochimie, 92, 1445-1453.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Burkholderia cepacia
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Subunits

Subunits Comment Organism
More three-dimensional structural model of BcPeh28A, combining mass spectrometry analysis, disulfide bridges mapping, and computational modelling, 2 different models, molecular dynamics simulations, overview Burkholderia cepacia

Synonyms

Synonyms Comment Organism
BcPeh28A
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Burkholderia cepacia
endoPG
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Burkholderia cepacia
endopolygalacturonase
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Burkholderia cepacia
More the enzyme belongs to the glycoside hydrolase family 28 Burkholderia cepacia

General Information

General Information Comment Organism
additional information architecture and the amino acid topology of the subsites involved in the catalysis and in the substrate binding specificity, overview Burkholderia cepacia
physiological function endopolygalacturonases are responsible for the hydrolysis of the non-esterified regions of pectins Burkholderia cepacia