Linked Life Data

6505672

Source:http://linkedlifedata.com/resource/pubmed/id/6505672

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1985-1-4
pubmed:abstractText
The ultraviolet irradiation of the yeast D-glyceraldehyde-3-phosphate dehydrogenase carboxymethylated at the active site Cys residues, as with the rabbit muscle enzyme, led to the formation of a fluorescent NAD derivative with an emission maximum at 410 nm. Similar results were obtained with the enzyme selectively carboxymethylated at only 2 of its 4 active site Cys residues. The binding of NAD+ to both the carboxymethylated enzymes is non-cooperative or only weakly negatively cooperative when determined by NAD+ quenching of the intrinsic protein fluorescence. However, determinations of the amount of fluorescent NAD derivative formed under different NAD+ concentrations show that both the carboxymethylated enzymes appeared to bind NAD+ with positive cooperativity as in the case of the binding of NAD+ to the native apoenzyme. This seems to suggest that the spatial positioning of the nicotinamide moiety at the active site of the irradiated enzyme resembles more closely that of the nicotinamide ring in the native holoenzyme as compared to the carboxymethylated enzymes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0253-5823
pubmed:author
pubmed:issnType
Print
pubmed:volume
27
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
800-10
pubmed:dateRevised
2009-5-29
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
The cooperative behavior of yeast D-glyceraldehyde-3-phosphate. Dehydrogenase as studied by the formation of the fluorescent NAD derivative.
pubmed:publicationType
Journal Article