D-malate dehydrogenase (decarboxylating)

Last updated
D-malate dehydrogenase (decarboxylating)
Identifiers
EC no. 1.1.1.83
CAS no. 37250-20-7
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
Search
PMC articles
PubMed articles
NCBI proteins

In enzymology, a D-malate dehydrogenase (decarboxylating) (EC 1.1.1.83) is an enzyme that catalyzes the chemical reaction

(R)-malate + NAD+ pyruvate + CO2 + NADH

Thus, the two substrates of this enzyme are (R)-malate and NAD+, whereas its 3 products are pyruvate, CO2, and NADH.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of a donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (R)-malate:NAD+ oxidoreductase (decarboxylating). Other names in common use include D-malate dehydrogenase, D-malic enzyme, bifunctional L(+)-tartrate dehydrogenase-D(+)-malate (decarboxylating). This enzyme participates in butanoate metabolism.

Related Research Articles

<span class="mw-page-title-main">Citric acid cycle</span> Chemical reactions to release energy in cells

The citric acid cycle —also known as the Krebs cycle, Szent-Györgyi-Krebs cycle or the TCA cycle (tricarboxylic acid cycle)—is a series of chemical reactions to release stored energy through the oxidation of acetyl-CoA derived from carbohydrates, fats, and proteins. The Krebs cycle is used by organisms that respire (as opposed to organisms that ferment) to generate energy, either by anaerobic respiration or aerobic respiration. In addition, the cycle provides precursors of certain amino acids, as well as the reducing agent NADH, that are used in numerous other reactions. Its central importance to many biochemical pathways suggests that it was one of the earliest components of metabolism. Even though it is branded as a 'cycle', it is not necessary for metabolites to follow only one specific route; at least three alternative segments of the citric acid cycle have been recognized.

<span class="mw-page-title-main">Oxaloacetic acid</span> Organic compound

Oxaloacetic acid (also known as oxalacetic acid or OAA) is a crystalline organic compound with the chemical formula HO2CC(O)CH2CO2H. Oxaloacetic acid, in the form of its conjugate base oxaloacetate, is a metabolic intermediate in many processes that occur in animals. It takes part in gluconeogenesis, the urea cycle, the glyoxylate cycle, amino acid synthesis, fatty acid synthesis and the citric acid cycle.

<span class="mw-page-title-main">Malate dehydrogenase</span> Class of enzymes

Malate dehydrogenase (EC 1.1.1.37) (MDH) is an enzyme that reversibly catalyzes the oxidation of malate to oxaloacetate using the reduction of NAD+ to NADH. This reaction is part of many metabolic pathways, including the citric acid cycle. Other malate dehydrogenases, which have other EC numbers and catalyze other reactions oxidizing malate, have qualified names like malate dehydrogenase (NADP+).

<span class="mw-page-title-main">Mitochondrial matrix</span> Space within the inner membrane of the mitochondrion

In the mitochondrion, the matrix is the space within the inner membrane. The word "matrix" stems from the fact that this space is viscous, compared to the relatively aqueous cytoplasm. The mitochondrial matrix contains the mitochondrial DNA, ribosomes, soluble enzymes, small organic molecules, nucleotide cofactors, and inorganic ions.[1] The enzymes in the matrix facilitate reactions responsible for the production of ATP, such as the citric acid cycle, oxidative phosphorylation, oxidation of pyruvate, and the beta oxidation of fatty acids.

<span class="mw-page-title-main">Pyruvate dehydrogenase</span> Class of enzymes

Pyruvate dehydrogenase is an enzyme that catalyzes the reaction of pyruvate and a lipoamide to give the acetylated dihydrolipoamide and carbon dioxide. The conversion requires the coenzyme thiamine pyrophosphate.

In enzymology, a dimethylmalate dehydrogenase (EC 1.1.1.84) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Homoisocitrate dehydrogenase</span> Enzyme

In enzymology, a homoisocitrate dehydrogenase (EC 1.1.1.87) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Malate dehydrogenase (decarboxylating)</span> Enzyme

Malate dehydrogenase (decarboxylating) (EC 1.1.1.39) or NAD-malic enzyme (NAD-ME) is an enzyme that catalyzes the chemical reaction

Malate dehydrogenase (NADP<sup>+</sup>)

In enzymology, a malate dehydrogenase (NADP+) (EC 1.1.1.82) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Malate dehydrogenase (oxaloacetate-decarboxylating)</span>

In enzymology, a malate dehydrogenase (oxaloacetate-decarboxylating) (EC 1.1.1.38) is an enzyme that catalyzes the chemical reaction below

Malate dehydrogenase (oxaloacetate-decarboxylating) (NADP<sup>+</sup>) Enzyme

Malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+) (EC 1.1.1.40) or NADP-malic enzyme (NADP-ME) is an enzyme that catalyzes the chemical reaction in the presence of a bivalent metal ion:

In enzymology, a sterol-4alpha-carboxylate 3-dehydrogenase (decarboxylating) (EC 1.1.1.170) is an enzyme that catalyzes the chemical reaction

In enzymology, a 1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (EC 1.3.1.25) is an enzyme that catalyzes the chemical reaction

In enzymology, an arogenate dehydrogenase (EC 1.3.1.43) is an enzyme that catalyzes the chemical reaction

In enzymology, an arogenate dehydrogenase [NAD(P)+] (EC 1.3.1.79) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Prephenate dehydrogenase</span> Class of enzymes

Prephenate dehydrogenase is an enzyme found in the shikimate pathway, and helps catalyze the reaction from prephenate to tyrosine.

In enzymology, a terephthalate 1,2-cis-dihydrodiol dehydrogenase (EC 1.3.1.61) is an enzyme that catalyzes the chemical reaction:

Alanine dehydrogenase (EC 1.4.1.1) is an enzyme that catalyzes the chemical reaction

Glutaminolysis (glutamine + -lysis) is a series of biochemical reactions by which the amino acid glutamine is lysed to glutamate, aspartate, CO2, pyruvate, lactate, alanine and citrate.

Malate dehydrogenase is an enzyme that reversibly catalyzes the oxidation of malate to oxaloacetate using the reduction of NAD+ to NADH.

References