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M1567

Sigma-Aldrich

Malic Dehydrogenase from porcine heart

≥600 units/mg protein (biuret), ammonium sulfate suspension

Synonym(s):

L-Malate: NAD+ oxidoreductase, MDH, Malate Dehydrogenase

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About This Item

Enzyme Commission number:
1.1.1.37 (BRENDA, IUBMB)
EC Number:
232-622-5
MDL number:
MFCD00131567
UNSPSC Code:
12352204
NACRES:
NA.54

form

ammonium sulfate suspension

specific activity

≥600 units/mg protein (biuret)

foreign activity

Glutamic-Oxalacetic Transaminase ≤0.01%
Glutamic-Pyruvic Transaminase ≤0.01%

storage temp.

2-8°C

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General description

Malic Dehydrogenase is a ubiquitous enzyme, which exists in two isoforms in eukaryotic cells.
Malic dehydrogenase exists as a dimer with each subunit containing an NAD-binding domain and a substrate-binding carboxy-terminal domain required for activity.
Malic dehydrogenase is a cytoplasmic isozyme and an important catalyst in the tricarboxylic acid cycle.

Application

Malic Dehydrogenase from porcine heart has been used:
  • in qualitative protein binding measurements
  • to test internally calibrated electrochemical continuous enzyme assay (ICECEA) with model enzyme pair
  • to investigate the effect of chaperone on the refolding of heat-denatured malate dehydrogenase

Malic dehydrogenase has been used in a study to assess the effect of an immunomodulator S2 complex on the enzymes of the parasites. It has also been used in a study to investigate the heterogeneity of lactic and malic dehydrogenase in cerebrospinal fluid.

Biochem/physiol Actions

Malic Dehydrogenase (MDH) plays an important role in the citric acid cycle in mitochondria. It catalyzes the interconversion of substrates malate and oxaloacetate with the simultaneous oxidation/reduction of NAD/NADH+. MDH present in the cytosol is involved in the shuttling of malate/aspartate.

Unit Definition

One unit will convert 1.0 μmole of oxalacetate and β-NADH to L-malate and β-NAD per min at pH 7.5 at 25°C.

Physical form

Suspension in 2.8 M (NH4)2SO4 solution, pH 6.0

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

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Yassir M Al-Mulla Hummadi et al.
Experimental parasitology, 112(2), 85-91 (2005-11-09)
S(2) complex has been reported to have a direct antileishmanial effect. The possibility that the direct antileishmanial effect may be due to inhibition of key enzymes involved in glucose metabolism and/ or enzymes associated with virulence was investigated. Cell pellets
Heterogeneity of lactic and malic dehydrogenase in cerebrospinal fluid
Lowenthal, A., et al.
Journal of Neurochemistry, 7, 135-140 (2006)
Electrochemical Coupled-Enzyme Assays at Carbon Nanotubes
Zhang M, et al.
Analytical Chemistry, 86(18), 9330-9334 (2014)
Malate dehydrogenases-structure and function
Minarik P, et al.
General Physiology and Biophysics, 21(3), 257-266 (2002)
Sensing NADH conformation using phasor analysis on fluorescence spectra
Palo D, et al.
Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy, 186(3), 105-111 (2017)
View All Related Papers

Articles

How to Work with Enzymes Supplied as Ammonium Sulfate Suspensions

Instructions for working with enzymes supplied as ammonium sulfate suspensions

Protocols

Enzymatic Assay of Malic Dehydrogenase (EC 1.1.1.37)

Malic dehydrogenase from bovine heart contains a histidine residue at the NAD-binding active site that is critical for activity. This protocol uses a spectrophotometric assay to evaluate malic dehydrogenase activity.

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