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Literature summary for 3.1.1.86 extracted from

  • Langkilde, A.; Kristensen, S.M.; Lo Leggio, L.; Molgaard, A.; Jensen, J.H.; Houk, A.R.; Navarro Poulsen, J.C.; Kauppinen, S.; Larsen, S.
    Short strong hydrogen bonds in proteins: a case study of rhamnogalacturonan acetylesterase (2008), Acta Crystallogr. Sect. D, 64, 851-863.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
vapour-diffusion method, the crystal structure of rhamnogalacturonan acetylesterase D192N is determined to 1.33 A resolution and refined to an R value of 11.6% for all data. The structure is virtually identical to the high-resolution (1.12 A) structure of the wild-type enzyme except for the interactions involving the mutation and a disordered loop Aspergillus aculeatus

Organism

Organism UniProt Comment Textmining
Aspergillus aculeatus Q00017
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Synonyms

Synonyms Comment Organism
RGAE
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Aspergillus aculeatus