1e71

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Template:STRUCTURE 1e71

File:1e71.png

MYROSINASE FROM SINAPIS ALBA WITH BOUND ASCORBATEMYROSINASE FROM SINAPIS ALBA WITH BOUND ASCORBATE

Template:ABSTRACT PUBMED 10978344

About this StructureAbout this Structure

1E71 is a 1 chain structure of sequence from Sinapis alba. Full crystallographic information is available from OCA.

ReferenceReference

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↑ Burmeister WP, Cottaz S, Rollin P, Vasella A, Henrissat B. High resolution X-ray crystallography shows that ascorbate is a cofactor for myrosinase and substitutes for the function of the catalytic base. J Biol Chem. 2000 Dec 15;275(50):39385-93. PMID:10978344 doi:http://dx.doi.org/10.1074/jbc.M006796200
↑ Burmeister WP, Cottaz S, Driguez H, Iori R, Palmieri S, Henrissat B. The crystal structures of Sinapis alba myrosinase and a covalent glycosyl-enzyme intermediate provide insights into the substrate recognition and active-site machinery of an S-glycosidase. Structure. 1997 May 15;5(5):663-75. PMID:9195886

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OCA

[1] Burmeister WP, Cottaz S, Rollin P, Vasella A, Henrissat B. High resolution X-ray crystallography shows that ascorbate is a cofactor for myrosinase and substitutes for the function of the catalytic base. J Biol Chem. 2000 Dec 15;275(50):39385-93. PMID:10978344 doi:http://dx.doi.org/10.1074/jbc.M006796200

[2] Burmeister WP, Cottaz S, Driguez H, Iori R, Palmieri S, Henrissat B. The crystal structures of Sinapis alba myrosinase and a covalent glycosyl-enzyme intermediate provide insights into the substrate recognition and active-site machinery of an S-glycosidase. Structure. 1997 May 15;5(5):663-75. PMID:9195886

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