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LMDH-RO

Roche

L-Malate Dehydrogenase (L-MDH)

from pig heart (mitochondrial)

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Enzyme Commission number:
1.1.1.37 (BRENDA, IUBMB)
UNSPSC Code:
12352200

biological source

Porcine heart (mitochondrial)

Quality Level

100

form

solution
suspension

specific activity

~1200 units/mg protein (At 25 °C with oxaloacetate as the substrate.)

packaging

pkg of 1 mL (10127248001 solution)
pkg of 1 mL (10127256001 suspension)
pkg of 5 mL (10127914001suspension)

manufacturer/tradename

Roche

technique(s)

activity assay: suitable

color

white

optimum pH

7.4-7.5(reduction of oxaloacetate)
9.2-9.5(oxidation of malate)

solubility

water: miscible

suitability

suitable for Western blot

NCBI accession no.

NM_001244153.1

UniProt accession no.

P00346

application(s)

life science and biopharma

foreign activity

Fumarase <0.01%
GIDH 0.001%
GOT 0.001%
GPT 0.00185%
LDH <0.01%
NADH oxidase <0.001%

shipped in

wet ice

storage temp.

2-8°C

Gene Information

Porcine ... MDH2(397039)

Related Categories

General description

L-malate:NAD+ oxidoreductase
The L-malate dehydrogenase enzyme is a nuclear gene product that is synthesized with a 24-residue amino-terminal signal peptide. This peptide is proteolytically cleaved during the translocation of the enzyme to the mitochondrial matrix.

Application

The enzyme L-malate dehydrogenase from pig heart has been used to measure PEPCK (phosphoenolpyruvate carboxykinase) activity. The oxaloacetate, produced by PEPCK, is reduced to malate via the oxidation of NADH, which in turn is measured at 340 nm using a spectrophotometer. The enzyme has also been used to measure oxaloacetate by measuring the reduction in NADH spectroscopically at 340 nm.

Biochem/physiol Actions

The enzyme L-malate dehydrogenase from pig heart catalyzes the oxidation of L-malate to oxaloacetate. The enzyme is an NAD-dependent mitochondrial dehydrogenase that functions in the tricarboxylic acid cycle. It is a component of the malate-aspartate shuttle that transports reducing equivalents across the inner mitochondrial membrane in the form of malate.

Quality

Contaminants: <0.002% GOT, <0.01% fumarase and LDH, each luM each, <0.02% HK, <0.002% PGI

Physical form

Solution in 50% glycerol (v/v), pH approximately 7
Suspension in 3.2 M ammonium sulfate solution, pH approximately 6

Preparation Note

Activator: – phosphate
– arsenate
– Mg2+
– Zn2+

Other Notes

For life science research only. Not for use in diagnostic procedures.

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 1

Flash Point(F)

No data available

Flash Point(C)

No data available

Regulatory Information

动植物源性产品

Certificates of Analysis (COA)

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Extraction and Measurement the Activities of Cytosolic Phosphoenolpyruvate Carboxykinase (PEPCK) and Plastidic NADP-dependent Malic Enzyme (ME) on Tomato (Solanum lycopersicum).
Osorio, S et al.
Bio-protocol, 4 (2014)
Agata M Pudlik et al.
Journal of bacteriology, 193(3), 706-714 (2010-12-01)
Carbohydrate/citrate cometabolism in Lactococcus lactis results in the formation of the flavor compound acetoin. Resting cells of strain IL1403(pFL3) rapidly consumed citrate while producing acetoin when substoichiometric concentrations of glucose or l-lactate were present. A proton motive force was generated
S L Roderick et al.
The Journal of biological chemistry, 261(20), 9461-9464 (1986-07-15)
In a previous study, we reported the apparent similarity between a low resolution electron density map of mitochondrial malate dehydrogenase and a model of cytoplasmic malate dehydrogenase (Roderick, S. L., and Banaszak, L. J. (1983) J. Biol. Chem. 258, 11636-11642).

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