1e73: Difference between revisions
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[[Image:1e73.png|left|200px]] | [[Image:1e73.png|left|200px]] | ||
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==About this Structure== | ==About this Structure== | ||
[[1e73]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Sinapis_alba Sinapis alba]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E73 OCA]. | |||
==Reference== | ==Reference== | ||
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[[Category: Thioglucosidase]] | [[Category: Thioglucosidase]] | ||
[[Category: Burmeister, W P.]] | [[Category: Burmeister, W P.]] | ||
Revision as of 07:49, 16 February 2011
2-F-GLUCOSYLATED MYROSINASE FROM SINAPIS ALBA WITH BOUND L-ASCORBATE2-F-GLUCOSYLATED MYROSINASE FROM SINAPIS ALBA WITH BOUND L-ASCORBATE
Template:ABSTRACT PUBMED 10978344
About this StructureAbout this Structure
1e73 is a 1 chain structure with 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