Many flavin reductases and monooxygenases bind NAD(P)H without the Rossmann fold. See the review by Massey (2000) The chemical and biological versatility of riboflavin. Biochem. Soc. Trans. 28(4):283-296. Also, ALDHs bind NAD(P)+ with a Rossmann-like fold, which is considered to be a nonclassical Rossmann fold. See Liu, et al., Nat. Struct. Biol. 1997.
On Aug 12, 2012, at 3:20 PM, Karsten Niefind wrote: > 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
