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Literature summary for 3.2.1.147 extracted from

  • Burmeister, W.P.; Cottaz, S.; Driguez, H.; Iori, R.; Palmieri, S.; Henrissat, B.
    The crystal structures of Sinapis alba myrosinase and a covalent glycosyl-enzyme intermediate provide insight into the substrate recognition and active-site machinery of an S-glycosidase (1997), Structure, 5, 663-675.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
native myrosinase and stable glycosyl-enzyme intermediate Sinapis alba

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ dimeric enzyme is stabilized by a Zn2+-ion bound on a twofold axis. The Zn2+ has a tetrahedral coordination, with angles between 97° and 118°, though four residues: His56 and Asp70, and their symmetry-related equivalents Sinapis alba

Organism

Organism UniProt Comment Textmining
Sinapis alba
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-
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Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein contains 13000 Da carbohydrate per dimer, the carbohydrate is required to maintain molecular stability and solubility in the dehydrated environment of the seed Sinapis alba

Source Tissue

Source Tissue Comment Organism Textmining
seed
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Sinapis alba
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
sinigrin + H2O
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Sinapis alba D-glucose + 3-isothiocyanatoprop-1-ene + SO42-
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