Linked Life Data

16662959

Source:http://linkedlifedata.com/resource/pubmed/id/16662959

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2010-6-29
pubmed:abstractText
Glycine decarboxylase has been successfully solubilized from pea (Pisum sativum) leaf mitochondria as an acetone powder. The enzyme was dependent on added dithiothreitol and pyridoxal phosphate for maximal activity. The enzyme preparation could catalyze the exchange of CO(2) into the carboxyl carbon of glycine, the reverse of the glycine decarboxylase reaction by converting serine, NH(4) (+), and CO(2) into glycine, and (14)CO(2) release from [1-(14)C]glycine. The half-maximal concentrations for the glycine-bicarbonate exchange reaction were 1.7 millimolar glycine, 16 millimolar NaH(14)CO(2), and 0.006 millimolar pyridoxal phosphate. The enzyme (glycine-bicarbonate exchange reaction) was active in the assay conditions for 1 hour and could be stored for over 1 month. The enzymic mechanism appeared similar to that reported for the enzyme from animals and bacteria but some quantitative differences were noted. These included the tenacity of binding to the mitochondrial membrane, the concentration of pyridoxal phosphate needed for maximum activity, the requirement for dithiothreitol for maximum activity, and the total amount of activity present. Now that this enzyme has been solubilized, a more detailed understanding of this important step in photorespiration should be possible.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:status
PubMed-not-MEDLINE
pubmed:month
May
pubmed:issn
0032-0889
pubmed:author
pubmed:issnType
Print
pubmed:volume
72
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
194-9
pubmed:dateRevised
2010-9-14
pubmed:year
1983
pubmed:articleTitle
Extraction and partial characterization of the glycine decarboxylase multienzyme complex from pea leaf mitochondria.
pubmed:affiliation
Department of Bacteriology and Biochemistry, University of Idaho, Moscow, Idaho 83843.
pubmed:publicationType
Journal Article