1e71: Difference between revisions
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==Reference== | ==Reference== | ||
<ref group="xtra">PMID: | <ref group="xtra">PMID:010978344</ref><ref group="xtra">PMID:009195886</ref><references group="xtra"/> | ||
[[Category: Sinapis alba]] | [[Category: Sinapis alba]] | ||
[[Category: Thioglucosidase]] | [[Category: Thioglucosidase]] | ||
[[Category: Burmeister, W P.]] | [[Category: Burmeister, W P.]] | ||
[[Category: Activation]] | [[Category: Activation]] | ||
[[Category: Family 1 glycosyl hydrolase]] | [[Category: Family 1 glycosyl hydrolase]] | ||
[[Category: Glucosinolate]] | [[Category: Glucosinolate]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Tim barrel]] | [[Category: Tim barrel]] | ||
Revision as of 05:33, 30 November 2011
MYROSINASE FROM SINAPIS ALBA WITH BOUND ASCORBATE
Template:ABSTRACT PUBMED 10978344
About this Structure
1e71 is a 1 chain structure with sequence from Sinapis alba. Full crystallographic information is available from OCA.
Reference
- 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:https://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
