"Malate Dehydrogenase" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
An enzyme that catalyzes the conversion of (S)-malate and NAD+ to oxaloacetate and NADH. EC 1.1.1.37.
| Descriptor ID |
D008291
|
| MeSH Number(s) |
D08.811.682.047.820.496
|
| Concept/Terms |
Malate Dehydrogenase- Malate Dehydrogenase
- Dehydrogenase, Malate
- NAD-Malate Dehydrogenase
- Dehydrogenase, NAD-Malate
- NAD Malate Dehydrogenase
- Malic Dehydrogenase
- Dehydrogenase, Malic
|
Below are MeSH descriptors whose meaning is more general than "Malate Dehydrogenase".
Below are MeSH descriptors whose meaning is more specific than "Malate Dehydrogenase".
This graph shows the total number of publications written about "Malate Dehydrogenase" by people in this website by year, and whether "Malate Dehydrogenase" was a major or minor topic of these publications.
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click here.
| Year | Major Topic | Minor Topic | Total |
|---|
| 1994 | 1 | 0 | 1 |
| 1995 | 1 | 0 | 1 |
| 1996 | 1 | 0 | 1 |
| 1997 | 1 | 0 | 1 |
| 1998 | 1 | 1 | 2 |
| 1999 | 2 | 0 | 2 |
| 2000 | 2 | 0 | 2 |
| 2002 | 2 | 0 | 2 |
| 2003 | 2 | 0 | 2 |
| 2005 | 1 | 0 | 1 |
| 2007 | 1 | 0 | 1 |
| 2008 | 2 | 0 | 2 |
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Below are the most recent publications written about "Malate Dehydrogenase" by people in Profiles.
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Role of residues in the adenosine binding site of NAD of the Ascaris suum malic enzyme. Biochim Biophys Acta. 2008 Dec; 1784(12):2059-64.
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Proper positioning of the nicotinamide ring is crucial for the Ascaris suum malic enzyme reaction. Biochemistry. 2008 Feb 26; 47(8):2539-46.
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Multiple roles of arginine 181 in binding and catalysis in the NAD-malic enzyme from Ascaris suum. Biochemistry. 2007 Dec 18; 46(50):14578-88.
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A catalytic triad is responsible for acid-base chemistry in the Ascaris suum NAD-malic enzyme. Biochemistry. 2005 Mar 08; 44(9):3626-35.
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Ascaris suum NAD-malic enzyme is activated by L-malate and fumarate binding to separate allosteric sites. Biochemistry. 2003 Aug 19; 42(32):9712-21.
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Crystallographic studies on Ascaris suum NAD-malic enzyme bound to reduced cofactor and identification of an effector site. J Biol Chem. 2003 Sep 26; 278(39):38051-8.
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Alternative substrates for malic enzyme: oxidative decarboxylation of L-aspartate. Biochemistry. 2002 Oct 08; 41(40):12200-3.
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Crystal structure of the malic enzyme from Ascaris suum complexed with nicotinamide adenine dinucleotide at 2.3 A resolution. Biochemistry. 2002 Jun 04; 41(22):6928-38.
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Lysine 199 is the general acid in the NAD-malic enzyme reaction. Biochemistry. 2000 Oct 03; 39(39):11955-60.
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Tumor grade, microvessel density, and activities of malate dehydrogenase, lactate dehydrogenase, and hexokinase in squamous cell carcinoma. Otolaryngol Head Neck Surg. 2000 Feb; 122(2):195-200.