3v0s
From Proteopedia
Contents |
Crystal Structure of Perakine Reductase, Founder Member of a Novel AKR Subfamily with Unique Conformational Changes during NADPH Binding
Template:ABSTRACT PUBMED 22334702
Function
[PERR_RAUSE] Aldo-keto reductase involved in the biosynthesis of monoterpenoid indole alkaloids. Broad substrate specificity enzyme with a high selectivity in the group of alkaloids. Can use perakine, 19(S),20(R)-dihydro-peraksine-17,21-al, cinnamic aldehyde, p-coumaric aldehyde and 3-(3,4,5-trimethoxyphenyl)propanal as substrates, but not ketosteroids such as progesterone. NADPH could not be replaced by NADH.[1]
About this Structure
3v0s is a 1 chain structure with sequence from Rauvolfia serpentina. Full crystallographic information is available from OCA.
Reference
- Sun L, Chen Y, Rajendran C, Mueller U, Panjikar S, Wang M, Mindnich R, Rosenthal C, Penning TM, Stockigt J. Crystal structure of perakine reductase, founding member of a novel aldo-keto reductase (AKR) subfamily that undergoes unique conformational changes during NADPH binding. J Biol Chem. 2012 Mar 30;287(14):11213-21. Epub 2012 Feb 13. PMID:22334702 doi:10.1074/jbc.M111.335521
- ↑ Sun L, Ruppert M, Sheludko Y, Warzecha H, Zhao Y, Stockigt J. Purification, cloning, functional expression and characterization of perakine reductase: the first example from the AKR enzyme family, extending the alkaloidal network of the plant Rauvolfia. Plant Mol Biol. 2008 Jul;67(5):455-67. doi: 10.1007/s11103-008-9331-7. Epub 2008 , Apr 13. PMID:18409028 doi:10.1007/s11103-008-9331-7
