1e71: Difference between revisions
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==Reference== | ==Reference== | ||
<ref group="xtra">PMID:10978344</ref><references group="xtra"/> | <ref group="xtra">PMID:10978344</ref><ref group="xtra">PMID:9195886</ref><references group="xtra"/> | ||
[[Category: Sinapis alba]] | [[Category: Sinapis alba]] | ||
[[Category: Thioglucosidase]] | [[Category: Thioglucosidase]] | ||
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[[Category: Family 1 glycosyl hydrolase]] | [[Category: Family 1 glycosyl hydrolase]] | ||
[[Category: Glucosinolate]] | [[Category: Glucosinolate]] | ||
[[Category: Hydrolase]] | |||
[[Category: Myrosinase]] | [[Category: Myrosinase]] | ||
[[Category: Tim barrel]] | [[Category: Tim barrel]] | ||
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Revision as of 09:08, 17 June 2009
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
- ↑ 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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