1e4m
From Proteopedia
(Difference between revisions)
m (Protected "1e4m" [edit=sysop:move=sysop]) |
|||
| Line 22: | Line 22: | ||
==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]] | ||
| Line 29: | Line 29: | ||
[[Category: Glucosinolate]] | [[Category: Glucosinolate]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
| - | [[Category: Myrosinase]] | ||
[[Category: Tim barrel]] | [[Category: Tim barrel]] | ||
Revision as of 10:58, 9 November 2011
MYROSINASE FROM SINAPIS ALBA
Template:ABSTRACT PUBMED 10978344
About this Structure
1e4m 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: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
