Linked Life Data

4719907

Source:http://linkedlifedata.com/resource/pubmed/id/4719907

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
97
pubmed:dateCreated
1973-9-26
pubmed:abstractText
The enzyme, 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase, catalyzes several reactions, the natural ones being (i) the exchange of hydrogen atoms of the methyl groups of pyruvate with protons of the solvent (C-H synthesis) and (ii) the reversible condensation of pyruvate with D-glyceraldehyde-3-phosphate (C-C synthesis). Previous work has provided chemical evidence for the occurrence of a protein-bound carboxylate group adjacent to the Schiff's base-forming lysine in the active site geometry. This carboxylate could provide the basic group postulated to participate in proton activation catalyzed by aldolases. With the use of three-dimensional models, it is shown that simple rotation about a carbon-carbon bond of the side chain will allow the base to assume the two positions necessary for proton activation in either the C-H synthesis or the C-C synthesis catalyzed by KDPG aldolase. This single base hypothesis provides a model wherein all reagents can approach a single face of the active site and is consistent with the stereochemistry thought to occur in the aldolase reaction.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0036-8075
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
181
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
350-2
pubmed:dateRevised
2007-8-17
pubmed:meshHeading
pubmed:year
1973
pubmed:articleTitle
Aldolase catalysis: single base-mediated proton activation.
pubmed:publicationType
Journal Article