EBI Databases InterPro	Search Open in usermanual InterPro:
Jump to: InterProScan Databases Documentation FTP site Help Click on the icon for context sensitive help from the user manual. Advanced search

InterPro: IPR001252 Malate dehydrogenase, active site

Protein matches Help

UniProtKB

Matches:

2140 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR001252 Malate_DH_AS

Type

Active_site

Signatures Help

Database	ID	Name	Proteins
PROSITE pattern	PS00068	MDH	2140
Signatures in BioMart

InterPro Relationships Help

Found in

IPR001236 Lactate/malate dehydrogenase
IPR010097 Malate dehydrogenase, NAD-dependent, eukaryote/gamma proteobacteria
IPR010945 Malate dehydrogenase, NAD/NADP
IPR011273 Malate dehydrogenase, NADP-dependent, plants
IPR011274 Malate dehydrogenase, NAD-dependent, cytosolic
IPR015955 Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal

GO Term annotation Help

Process

GO:0006108 malate metabolic process
GO:0055114 oxidation reduction

Function

GO:0016615 malate dehydrogenase activity

InterPro annotation

Entry Details in BioMart

Abstract

Malate dehydrogenase (EC:1.1.1.37) (MDH) [1] 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 specialised C4 cycle.

The pattern for this enzyme includes two residues involved in the catalytic mechanism [2]: an aspartic acid which is involved in a proton relay mechanism, and an arginine which binds the substrate.

Structural links Help

PDB - click here

SCOP: c.2.1.5 , d.162.1.1

CATH: 3.40.50.720 , 3.90.110.10

Database links Help

PDBe-motif: PS00068

Enzyme: EC:1.1.1.37

PROSITE doc: PDOC00066

Blocks: IPB001252

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR001252

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O02640 Probable malate dehydrogenase, mitochondrial

O82399 Probable malate dehydrogenase, glyoxysomal

P08249 Malate dehydrogenase, mitochondrial

P17505 Malate dehydrogenase, mitochondrial

P40926 Malate dehydrogenase, mitochondrial

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR001236	Lactate/malate dehydrogenase
IPR010097	Malate dehydrogenase, NAD-dependent, eukaryote/gamma proteobacteria
IPR016040	NAD(P)-binding domain
IPR001252	Malate dehydrogenase, active site
IPR001557	L-lactate/malate dehydrogenase
IPR015955	Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain

Publications Open in usermanual
1.	Gietl C. Malate dehydrogenase isoenzymes: cellular locations and role in the flow of metabolites between the cytoplasm and cell organelles. Biochim. Biophys. Acta 1100 217-34 1992 [PubMed: 1610875] http://dx.doi.org/10.1016/0167-4838(92)90476-T
2.	Birktoft JJ, Rhodes G, Banaszak LJ. Refined crystal structure of cytoplasmic malate dehydrogenase at 2.5-A resolution. Biochemistry 28 6065-81 1989 [PubMed: 2775751] http://dx.doi.org/10.1021/bi00440a051

Additional Reading Open in usermanual
	Johansson K, Ramaswamy S, Saarinen M, Lemaire-Chamley M, Issakidis-Bourguet E, Miginiac-Maslow M, Eklund H. Structural basis for light activation of a chloroplast enzyme: the structure of sorghum NADP-malate dehydrogenase in its oxidized form. Biochemistry 38 1999 4319-26 [PubMed: 10194350] http://dx.doi.org/10.1021/bi982876c
	Tomita T, Fushinobu S, Kuzuyama T, Nishiyama M. Crystal structure of NAD-dependent malate dehydrogenase complexed with NADP(H). Biochem. Biophys. Res. Commun. 334 2005 613-8 [PubMed: 16009341] http://dx.doi.org/10.1016/j.bbrc.2005.06.133
	Chapman AD, Cortes A, Dafforn TR, Clarke AR, Brady RL. Structural basis of substrate specificity in malate dehydrogenases: crystal structure of a ternary complex of porcine cytoplasmic malate dehydrogenase, alpha-ketomalonate and tetrahydoNAD. J. Mol. Biol. 285 1999 703-12 [PubMed: 10075524] http://dx.doi.org/10.1006/jmbi.1998.2357
	Cendrin F, Chroboczek J, Zaccai G, Eisenberg H, Mevarech M. Cloning, sequencing, and expression in Escherichia coli of the gene coding for malate dehydrogenase of the extremely halophilic archaebacterium Haloarcula marismortui. Biochemistry 32 1993 4308-13 [PubMed: 8476859] http://dx.doi.org/10.1021/bi00067a020
	Cox B, Chit MM, Weaver T, Gietl C, Bailey J, Bell E, Banaszak L. Organelle and translocatable forms of glyoxysomal malate dehydrogenase. The effect of the N-terminal presequence. FEBS J. 272 2005 643-54 [PubMed: 15670147] http://dx.doi.org/10.1111/j.1742-4658.2004.04475.x
	Bell JK, Yennawar HP, Wright SK, Thompson JR, Viola RE, Banaszak LJ. Structural analyses of a malate dehydrogenase with a variable active site. J. Biol. Chem. 276 2001 31156-62 [PubMed: 11389141] http://dx.doi.org/10.1074/jbc.M100902200

InterPro 23.1