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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
15
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pubmed:dateCreated |
1989-11-22
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pubmed:abstractText |
Substrate activation of the rate of the NAD-malic enzyme reaction by malate is obtained in the presence but not in the absence of oxalate. The substrate activation is a result of competition between malate and oxalate for the E.NADH complex, with malate binding to the form of the complex unprotonated at an enzyme group with a pK of 4.9 and oxalate binding preferentially to the protonated form. The off-rate for NADH from the E.NADH complex is completely rate limiting when the group with a pK of 4.9 is protonated but is only one of several rate-limiting steps when it is unprotonated [Kiick, D.M., Harris, B.G., & Cook, P.F. (1986) Biochemistry 25, 227]. The competition by malate with oxalate thus results in an overall increase in the off-rate for NADH as a result of binding to the unprotonated form of E.NADH. Consistent with the proposed mechanism, the deuterium isotope effect on V for the nonsubstrate-activating malate concentration range decreases from 1.6 in the absence of oxalate to 1.3 in the presence of a concentration of oxalate equal to its Kii. The rate equation for the oxalate-induced substrate activation by malate is derived and presented in the Appendix. Data are discussed in terms of the overall mechanism of the NAD-malic enzyme.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
28
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
6334-40
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:2790001-Animals,
pubmed-meshheading:2790001-Ascaris,
pubmed-meshheading:2790001-Enzyme Activation,
pubmed-meshheading:2790001-Kinetics,
pubmed-meshheading:2790001-Malate Dehydrogenase,
pubmed-meshheading:2790001-Malates,
pubmed-meshheading:2790001-Mathematics,
pubmed-meshheading:2790001-Mitochondria,
pubmed-meshheading:2790001-Models, Theoretical,
pubmed-meshheading:2790001-Oxalates
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pubmed:year |
1989
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pubmed:articleTitle |
Substrate activation by malate induced by oxalate in the Ascaris suum NAD-malic enzyme reaction.
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pubmed:affiliation |
Department of Biochemistry, Texas College of Osteopathic Medicine, Fort Worth.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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