Literature summary for 1.1.1.37 extracted from

Irimia, A.; Ebel, C.; Madern, D.; Richard, S.B.; Cosenza, L.W.; Zaccai, G.; Vellieux, F.M.
The oligomeric states of Haloarcula marismortui malate dehydrogenase are modulated by solvent components as shown by crystallographic and biochemical studies (2003), J. Mol. Biol., 326, 859-873.

Search for more literature for 1.1.1.37

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Haloarcula marismortui

Crystallization (Commentary)

Crystallization (Comment)	Organism
sitting drop reverse vapour diffusion method, crystal structure of the R207S/R292S mutant of malate dehydrogenase is solved at 1.95 A	Haloarcula marismortui

Protein Variants

Protein Variants	Comment	Organism
R207S/R292S	the numbering is not equivalent to the numbering of UniProt. The mutations, located at the dimer-dimer interface, disrupt two inter-dimeric salt bridge clusters that are essential for wild-type tetramer stabilisation. Association of active dimers into tetramers is weakened	Haloarcula marismortui

Organism

Organism	UniProt	Comment	Textmining
Haloarcula marismortui	Q07841	-	-
Haloarcula marismortui DSM 3752	Q07841	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Haloarcula marismortui

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
oxaloacetate + NADH + H+	-	Haloarcula marismortui	(S)-malate + NAD+	-	?
oxaloacetate + NADH + H+	-	Haloarcula marismortui DSM 3752	(S)-malate + NAD+	-	?

Subunits

Subunits	Comment	Organism
dimer	wild-type enzyme and R207S/R292S mutant enzyme can both exist as dimeric species depending on solvent conditions. F- and SO42-, as well as the NADH cofactor, stabilize the dimeric form of the wild-type protein	Haloarcula marismortui

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
20	-	assay at	Haloarcula marismortui

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8	-	assay at	Haloarcula marismortui

Cofactor

Cofactor	Comment	Organism	Structure
NADH	-	Haloarcula marismortui

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)