Search results for MDH2

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Species

Types

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Reaction types

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Protein (1 results from a total of 1)

Identifier: R-HSA-70977
Species: Homo sapiens
Compartment: mitochondrial matrix
Primary external reference: UniProt: MDH2: P40926

Complex (1 results from a total of 1)

Identifier: R-HSA-198511
Species: Homo sapiens
Compartment: mitochondrial matrix

Reaction (3 results from a total of 3)

Identifier: R-HSA-70979
Species: Homo sapiens
Compartment: mitochondrial matrix
Mitochondrial malate dehydrogenase (MDH2) dimer catalyzes the reversible reaction of malate and NAD+ to form oxaloacetate (OA) and NADH + H+ (Luo et al. 2006; Eo et al., 2022). This reaction is highly endergonic but is pulled in the direction annotated here when the TCA cycle is operating. The active enzyme is a palmitoylated homodimer (Sanchez et al. 1998; Pei et al., 2022). Mutations in MDH2 can cause infantile epileptic encephalopathy (DEE51, MIM:617339; see Priestley et al., 2022).
Identifier: R-HSA-9856871
Species: Homo sapiens
Compartment: cytosol
Cytosolic MDH1 (malate dehydrogenase 1) catalyzes the reversible reaction of oxaloacetate (OA) and NADH + H+ to form malate (MAL) and NAD+ (Friedrich et al. 1988; Lo et al. 2005). This reaction provides the malate-aspartate shuttle with reducing equivalents that are transported in the form of MAL into the mitochondrion, and are available there as NADH from the reverse reaction catalyzed by MDH2. Sources of cytosolic NADH are glycolysis, serine biosynthesis, and peroxisomal fatty acid oxidation (reviewed by Borst, 2020). The dimeric structure of the human dehydrogenase is inferred from human and pig crystallographic data (McCue & Finzel, 2021; Birktoft et al. 1989). Mutations in MDH1 can cause a form of early-onset epileptic encephalopathy (DEE88, MIM:618959; Broeks et al., 2019).
Identifier: R-HSA-70975
Species: Homo sapiens
Compartment: mitochondrial matrix
Mitochondrial citrate synthase (CS) dimer catalyzes the irreversible reaction of acetyl-CoA, water, and oxaloacetate to form citrate and coenzyme A. This reaction is the entry point of two-carbon units into the citric acid cycle. The reaction is subject to allosteric regulation. Most of the time, CS is trimethylated on Lys-395 which attenuates its enzymatic activity (Malecki et al. 2017). The gene encoding the human enzyme has been cloned (Goldenthal et al. 1998), but the enzyme has not been characterized in detail. Its properties are inferred from those of the well-studied homologous pig enzyme (e.g., Morgunov and Srere 1998).

CS dimer, malate dehydrogenase MDH2, and aconitase ACO2 form a multienzyme complex ("metabolon") that optimally channels the substrate flow between them (Fahien & Kmiotek, 1983; Wu & Minteer, 2014; Omini et al., 2021).
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