Linked Life Data

6853502

Source:http://linkedlifedata.com/resource/pubmed/id/6853502

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
1983-7-15
pubmed:abstractText
The substrate specificity of chalcone synthase, the key enzyme of flavonoid biosynthesis, was investigated. A purified enzyme preparation from cell suspension cultures of parsley (Petroselinum hortense) catalyzed chain elongations with acetate units from malonyl-CoA, using various aromatic and aliphatic CoA esters as starter molecules. Malonyl-CoA could not be replaced by malonyl acyl carrier protein in the standard chalcone synthase assay. Butyryl-CoA, hexanoyl-CoA, and benzoyl-CoA served as substrates for the condensation reaction with similar efficiency as 4-coumaroyl-CoA, the natural substrate of the enzyme. Acetyl-CoA and octanoyl-CoA were relatively poor substrates. Among the products formed with the two most efficient aliphatic substrates tested, butyryl-CoA and hexanoyl-CoA, were the respective chalcone analogues, phlorobutyrophenone and phlorocaprophenone. The possibility is discussed that chalcone synthase and the corresponding enzyme of fatty acid synthesis in higher plants, beta-ketoacyl-acyl carrier protein synthase, have a common evolutionary origin.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
258
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6730-4
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Substrate specificity of chalcone synthase from Petroselinum hortense. Formation of phloroglucinol derivatives from aliphatic substrates.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't