Enzyme

Download
EC Tree
     1. Oxidoreductases
        1.1 Acting on the CH-OH group of donors
            1.1.1 With NAD+ or NADP+ as acceptor
ID:1.1.1.331
Description:Secoisolariciresinol dehydrogenase.
Cath: 3.40.50.720;

3D structure

Click one PDB to see exact 3D structure provided by NGL.

Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.

References

External Links

UniProtKB Enzyme Link: UniProtKB 1.1.1.331
BRENDA Enzyme Link: BRENDA 1.1.1.331
KEGG Enzyme Link: KEGG1.1.1.331
BioCyc Enzyme Link: BioCyc 1.1.1.331
ExPASy Enzyme Link: ExPASy1.1.1.331
EC2PDB Enzyme Link: EC2PDB 1.1.1.331
ExplorEnz Enzyme Link: ExplorEnz 1.1.1.331
PRIAM enzyme-specific profiles Link: PRIAM 1.1.1.331
IntEnz Enzyme Link: IntEnz 1.1.1.331
MEDLINE Enzyme Link: MEDLINE 1.1.1.331
MSA:

1.1.1.331;

Phylogenetic Tree:

1.1.1.331;

Uniprot:
M-CSA:
RHEA:33887 (-)-secoisolariciresinol + 2 NAD(+) = (-)-matairesinol + 2 H(+) + 2 NADH
RULE(radius=1) ([*:1]-[CH2;+0:2]-[OH;+0:3].[*:4]-[OH;+0:5]).[*:6]-[c;H0;+0:7]1:[cH;+0:8]:[cH;+0:9]:[cH;+0:10]:[n+;H0:11](-[*:12]):[cH;+0:13]:1.[*:14]-[n+;H0:15]1:[cH;+0:16]:[cH;+0:17]:[cH;+0:18]:[c;H0;+0:19](-[*:20]):[cH;+0:21]:1>>[*:6]-[C;H0;+0:7]1=[CH;+0:13]-[N;H0;+0:11](-[*:12])-[CH;+0:10]=[CH;+0:9]-[CH2;+0:8]-1.[*:14]-[N;H0;+0:15]1-[CH;+0:16]=[CH;+0:17]-[CH2;+0:18]-[C;H0;+0:19](-[*:20])=[CH;+0:21]-1.[*:4]-[O;H0;+0:5]-[C;H0;+0:2](-[*:1])=[O;H0;+0:3]
Reaction
Core-to-Core More
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Secoisolariciresinol dehydrogenase: mode of catalysis and stereospecificity of hydride transfer in Podophyllum peltatum.Moinuddin SG, Youn B, Bedgar DL, Costa MA, Helms GL, Kang C, Davin LB, Lewis NG2006 Mar 716493463
Crystal structures of apo-form and binary/ternary complexes of Podophyllum secoisolariciresinol dehydrogenase, an enzyme involved in formation of health-protecting and plant defense lignans.Youn B, Moinuddin SG, Davin LB, Lewis NG, Kang C2005 Apr 115653677
Secoisolariciresinol dehydrogenase purification, cloning, and functional expression. Implications for human health protection.Xia ZQ, Costa MA, Pelissier HC, Davin LB, Lewis NG2001 Apr 2011278426