Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
25
pubmed:dateCreated
1986-3-26
pubmed:abstractText
4'-Phosphopantothenoyl-L-cysteine decarboxylase (PPC decarboxylase) was partially purified from rat liver. 4'-Phosphopantothenoyl[2-2H1]-L-cysteine was synthesized and converted by PPC decarboxylase to 4'-phosphol[1-2H1]pantetheine. The product was degraded by reduction with Raney nickel followed by acidic hydrolysis to [1-2H1]ethylamine. The latter was converted to the (-)-camphanamide derivative, NMR studies of which revealed that the deuterium was located in the pro-1S position. Also, unlabeled 4'-phosphopantothenoyl-L-cysteine was incubated with PPC decarboxylase in D2O, giving, after degradation, the (-)-camphanamide of (1R)-[1-2H1]ethylamine. The results show that the decarboxylation takes place with retention of configuration. These results are discussed in terms of possible mechanisms for the decarboxylation.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
24
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7178-82
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1985
pubmed:articleTitle
Coenzyme A biosynthesis: steric course of 4'-phosphopantothenoyl-L-cysteine decarboxylase.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.