Linked Life Data

6732801

Source:http://linkedlifedata.com/resource/pubmed/id/6732801

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1984-7-9
pubmed:abstractText
The substrate stereospecificity of 1- aminocyclopropane -1-carboxylic acid synthase, a pyridoxal phosphate-containing enzyme, from the pericarp tissue of Lycopersicon esculentum (tomatoes) was studied using the various stereoisomers of S-adenosylmethionine (AdoMet) at both the sulfonium pole and the amino acid center. The data indicate that only the naturally occurring isomer (-)Ado-L-Met acts as substrate (Km = 20 +/- 5 microM). Both (+/-)Ado-D-Met and (+)Ado-L-Met were inactive as substrates. The (+)Ado-L-Met (Ki = 15 +/- 5 microM) was found to be a potent inhibitor of ACC synthase whereas (+/-)Ado-D-Met (Ki = 70 +/- 20 microM) was less active as an inhibitor. This active isomer has the (S) configuration at both the sulfur and the alpha-carbon of the amino acid portion of AdoMet.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
31
pubmed:volume
121
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
181-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Stereochemical course of the biosynthesis of 1-aminocyclopropane-1-carboxylic acid. I. Role of the asymmetric sulfonium pole and the alpha-amino acid center.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't