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PROSITE documentation PDOC00066Malate dehydrogenase active site signature
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PURL: https://purl.expasy.org/prosite/documentation/PDOC00066
Malate dehydrogenase (EC 1.1.1.37) (MDH) [1,2] catalyzes the interconversion of malate to oxaloacetate utilizing the NAD/NADH cofactor system. The enzyme participates in the citric acid cycle and exists in all aerobics organisms.
While prokaryotic organisms contains a single form of MDH, in eukaryotic cells there are two isozymes: one which is located in the mitochondrial matrix and the other in the cytoplasm. Fungi and plants also harbor a glyoxysomal form which functions in the glyoxylate pathway. In plants chloroplast there is an additional NADP-dependent form of MDH (EC 1.1.1.82) which is essential for both the universal C3 photosynthesis (Calvin) cycle and the more specialized C4 cycle.
As a signature pattern for this enzyme we have chosen a region that includes two residues involved in the catalytic mechanism [3]: an aspartic acid which is involved in a proton relay mechanism, and an arginine which binds the substrate.
Note:MDH from archaebacteria do not belong to the above family; they are evolutionary related to lactate dehydrogenases [4].
Last update:November 1995 / Text revised.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | McAlister-Henn L. |
| Source | Trends Biochem. Sci. 13:178-181(1988). |
| 2 | Authors | Gietl C. |
| Title | Malate dehydrogenase isoenzymes: cellular locations and role in the flow of metabolites between the cytoplasm and cell organelles. | |
| Source | Biochim. Biophys. Acta 1100:217-234(1992). | |
| PubMed ID | 1610875 |
| 3 | Authors | Birktoft J.J. Rhodes G. Banaszak L.J. |
| Title | Refined crystal structure of cytoplasmic malate dehydrogenase at 2.5-A resolution. | |
| Source | Biochemistry 28:6065-6081(1989). | |
| PubMed ID | 2775751 |
| 4 | Authors | Cendrin F. Chroboczek J. Zaccai G. Eisenberg H. Mevarech M. |
| Title | Cloning, sequencing, and expression in Escherichia coli of the gene coding for malate dehydrogenase of the extremely halophilic archaebacterium Haloarcula marismortui. | |
| Source | Biochemistry 32:4308-4313(1993). | |
| PubMed ID | 8476859 |
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