Linked Life Data

3280016

Source:http://linkedlifedata.com/resource/pubmed/id/3280016

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1988-4-28
pubmed:abstractText
Isotope partitioning studies beginning with E.[14C]NAD, E.[14C]malate, E.[14C]NAD.Mg2+, and E.Mg.[14C]malate suggest a steady-state random mechanism for the NAD-malic enzyme. Isotope trapping beginning with E.[14C]NAD and with varying concentrations of Mg2+ and malate in the chase solution indicates that Mg2+ is added in rapid equilibrium and must be added prior to malate for productive ternary complex formation. Equal percentage trapping from E.[14C]NAD.Mg and E.Mg.[14C]malate indicates the mechanism is steady-state random with equal off-rates for NAD and malate from E.NAD.Mg.malate. The off-rates for both do not change significantly in the ternary E.Mg.malate and E.NAD.Mg complexes, nor does the off-rate change for NAD from E.NAD. No trapping of malate was obtained from E.[14C]malate, suggesting that this complex is nonproductive. A quantitative analysis of the data allows an estimation of values for a number of the rate constants along the reaction pathway.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
12
pubmed:volume
27
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
212-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Isotope partitioning for NAD-malic enzyme from Ascaris suum confirms a steady-state random kinetic mechanism.
pubmed:affiliation
Department of Biochemistry, Texas College of Osteopathic Medicine/North Texas State University, Denton 76203.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't