KEGG   ENZYME: 2.5.1.71Help
Entry
EC 2.5.1.71                 Enzyme                                 

Name
leachianone-G 2''-dimethylallyltransferase;
LG 2''-dimethylallyltransferase;
leachianone G 2''-dimethylallyltransferase;
LGDT
Class
Transferases;
Transferring alkyl or aryl groups, other than methyl groups;
Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)
BRITE hierarchy
Sysname
dimethylallyl-diphosphate:leachianone-G 2''-dimethylallyltransferase
Reaction(IUBMB)
dimethylallyl diphosphate + leachianone G = diphosphate + sophoraflavanone G [RN:R08952]
Reaction(KEGG)
Substrate
dimethylallyl diphosphate [CPD:C00235];
leachianone G [CPD:C18024]
Product
diphosphate [CPD:C00013];
sophoraflavanone G [CPD:C18053]
Comment
This membrane-bound enzyme is located in the plastids and requires Mg2+ for activity. The reaction forms the lavandulyl sidechain of sophoraflavanone G by transferring a dimethylallyl group to the 2'' position of another dimethylallyl group attached at postiion 8 of leachianone G. The enzyme is specific for dimethylallyl diphosphate as the prenyl donor, as it cannot be replaced by isopentenyl diphosphate or geranyl diphosphate. Euchrenone a7 (a 5-deoxy derivative of leachianone G) and kenusanone I (a 7-methoxy derivative of leachianone G) can also act as substrates, but more slowly. Along with EC 1.14.13.103 (8-dimethylallylnaringenin 2'-hydroxylase) and EC 2.5.1.70 (naringenin 8-dimethylallyltransferase), this enzyme forms part of the sophoraflavanone-G-biosynthesis pathway.
History
EC 2.5.1.71 created 2007
Reference
1  [PMID:14551337]
  Authors
Zhao P, Inoue K, Kouno I, Yamamoto H.
  Title
Characterization of leachianone G 2"-dimethylallyltransferase, a novel prenyl side-chain elongation enzyme for the formation of the lavandulyl group of sophoraflavanone G in Sophora flavescens Ait. cell suspension cultures.
  Journal
Plant. Physiol. 133 (2003) 1306-13.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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