Home | Contact

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.

MDH from archaebacteria do not belong to the above family; they are evolutionary related to lactate dehydrogenases [4].

November 1995 / Text revised.

PROSITE method (with tools and information) covered by this documentation:

MDH, PS00068; Malate dehydrogenase active site signature  (PATTERN)

Consensus pattern: [LIVM]-T-[TRKMN]-L-D-x(2)-R-[STA]-x(3)-[LIVMFY] D and R are the active site residues Sequences known to belong to this class detected by the pattern: ALL Other sequence(s) detected in Swiss-Prot: NONE.

• Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00068 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00068 • Scan Swiss-Prot/TrEMBL entries against PS00068 • view ligand binding statistics

Matching PDB structures: 1BDM 1BMD 1CIV 1CME ... [ALL]

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

PROSITE is copyright. It is produced by the SIB Swiss Institute Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified. Usage by and for commercial entities requires a license agreement. For information about the licensing scheme send an email to

Prosite License or see: prosite_license.html.


View entry in original PROSITE document format
View entry in raw text format (no links)

SIB Swiss Institute of Bioinformatics | Disclaimer