KEGG   ENZYME: 1.3.1.107Help
Entry
EC 1.3.1.107                Enzyme                                 

Name
sanguinarine reductase
Class
Oxidoreductases;
Acting on the CH-CH group of donors;
With NAD+ or NADP+ as acceptor
BRITE hierarchy
Sysname
dihydrosanguinarine:NAD(P)+ oxidoreductase
Reaction(IUBMB)
(1) dihydrosanguinarine + NAD(P)+ = sanguinarine + NAD(P)H + H+ [RN:R10798 R10799];
(2) dihydrochelirubine + NAD(P)+ = chelirubine + NAD(P)H + H+ [RN:R10800 R10801]
Reaction(KEGG)
Substrate
dihydrosanguinarine [CPD:C05191];
NAD+ [CPD:C00003];
NADP+ [CPD:C00006];
dihydrochelirubine [CPD:C05194]
Product
sanguinarine [CPD:C06162];
NADH [CPD:C00004];
NADPH [CPD:C00005];
H+ [CPD:C00080];
chelirubine [CPD:C06327]
Comment
The enzyme, purified from the California poppy (Eschscholzia californica), is involved in detoxifying the phytoalexin sanguinarine produced by poppy itself (cf. EC 1.5.3.12, dihydrobenzophenanthridine oxidase), when it binds to the cell wall of the poppy cell. The reaction with NADPH is up to three times faster than that with NADH at low concentrations (<10 uM) of the dinucleotide. At higher concentrations the reaction with NADPH is inhibited but not that with NADH [1].
History
EC 1.3.1.107 created 2014
Orthology
K20145  sanguinarine reductase
Reference
1  [PMID:17080644]
  Authors
Weiss D, Baumert A, Vogel M, Roos W
  Title
Sanguinarine reductase, a key enzyme of benzophenanthridine detoxification.
  Journal
Plant Cell Environ 29:291-302 (2006)
DOI:10.1111/j.1365-3040.2005.01421.x
Reference
2  [PMID:20378534]
  Authors
Vogel M, Lawson M, Sippl W, Conrad U, Roos W
  Title
Structure and mechanism of sanguinarine reductase, an enzyme of alkaloid detoxification.
  Journal
J Biol Chem 285:18397-406 (2010)
DOI:10.1074/jbc.M109.088989
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 1.3.1.107
IUBMB Enzyme Nomenclature: 1.3.1.107
ExPASy - ENZYME nomenclature database: 1.3.1.107
BRENDA, the Enzyme Database: 1.3.1.107

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