Zitat von Sudipta Bhattacharyya <sudiptabhattacharyya.iit...@gmail.com>:
Dear all,
I have biochemically characterized one enzyme that can dephosphorylate
NADP+ / NADPH. Recently, I have also solved the crystal structure of the
protein with bound NADP+. The important thing is that, the protein do not
have the Rossmann fold or the dinucleotide binding fold. Can any one please
cite or suggest any other example of such type of anomaly? Is there any
example of non-classical Rossmann fold bearing proteins?
Thanks,
Sudipta.
Dear Sudipta,
AKR enzymes (aldo/keto reductases; see www.med.upenn.edu/akr/ and
www.ncbi.nlm.nih.gov/pubmed/20887732) bind NAD(P) and have an
(alpha/beta)8 barrel motif.
Best wishes,
Karsten Niefind
-------------------------
Karsten Niefind, PhD
University of Cologne
Department of Chemistry
Otto-Fischer-Str. 12-14
D-50674 Cologne
Tel.: +49 (0)221 4706444
Fax: +49 (0)221 4703244
