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 <[log in to unmask]>:
>
>> 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
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