Search results for DLD

Showing 18 results out of 19

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Protein (5 results from a total of 5)

DLD

Identifier: R-HSA-69978
Species: Homo sapiens
Compartment: mitochondrial matrix
Primary external reference: UniProt: DLD: P09622
Identifier: R-HSA-1299433
Species: Homo sapiens
Compartment: mitochondrial inner membrane
Primary external reference: UniProt: LDHD: Q86WU2
The N-terminus of LDLD is predicted by software.
Identifier: R-HSA-1299437
Species: Homo sapiens
Compartment: mitochondrial inner membrane
Primary external reference: UniProt: LDHD: Q86WU2
Identifier: R-HSA-8986145
Species: Homo sapiens
Compartment: mitochondrial matrix
Primary external reference: UniProt: LDHD: Q86WU2
Identifier: R-HSA-1267974
Species: Homo sapiens
Compartment: mitochondrial intermembrane space
Primary external reference: UniProt: LDHD: Q86WU2

Complex (2 results from a total of 2)

Identifier: R-HSA-5694020
Species: Homo sapiens
Compartment: mitochondrial matrix
Identifier: R-HSA-69979
Species: Homo sapiens
Compartment: mitochondrial matrix

Reaction (6 results from a total of 7)

Identifier: R-HSA-9853499
Species: Homo sapiens
Compartment: mitochondrial matrix
Dihydrolipoyl dehydrogenase (DLD), the E3 component of the 2-oxoglutarate dehydrogenase metabolon, forms a homodimer that catalyzes the dehydrogenation of dihydrolipoyllysine residues by producing NADH from NAD+, with the help of the FAD cofactor (Brautigam et al., 2005). This reaction, in a side reaction not annotated here, is the main source of reactive oxygen species (ROS) in mitochondria (Ambrus et al., 2015). Deficiency of DLD activity due to mutations is a rare genetic disease (DLDD; MIM:246900; see Wongkittichote et al., 2023; reviewed in Ambrus & Adam-Viz, 2017).
Identifier: R-HSA-9861616
Species: Homo sapiens
Compartment: mitochondrial matrix
Dihydrolipoyl dehydrogenase (DLD), the E3 component of the 2-oxoglutarate dehydrogenase metabolon, forms a homodimer that catalyzes the dehydrogenation of dihydrolipoyllysine residues by producing NADH from NAD+, with the help of the FAD cofactor (Brautigam et al., 2005). This reaction, in a side reaction not annotated here, is the main source of reactive oxygen species (ROS) in mitochondria (Ambrus et al., 2015). Deficiency of DLD activity due to mutations is a rare genetic disease (DLDD; MIM:246900; see Wongkittichote et al., 2023; reviewed in Ambrus & Adam-Viz, 2017).
Identifier: R-HSA-5694018
Species: Homo sapiens
Compartment: mitochondrial matrix
The last step in the glycine cleavage system is the reoxidation of the reduced lipoate (dihydrolipoyl group) attached to the H protein (GCSH:DHLL) catalysed by the L protein (mitochondrial dihydrolipoyl dehydrogenase, DLD) (Harris et al. 1997, Ciszak et al. 2006).
Identifier: R-HSA-71037
Species: Homo sapiens
Compartment: mitochondrial matrix
The mitochondrial alpha-ketoglutarate dehydrogenase complex catalyzes the reaction of alpha-ketoadipate, CoASH, and NAD+ to form glutaryl-CoA, CO2, and NADH. The enzyme complex contains multiple copies of three different proteins, E1 (OGDH), E2 (DLST), and E3 (DLD), each with distinct catalytic activities (Reed and Hackert 1990; Zhou et al 2001). The reaction starts with the oxidative decarboxylation of alpha-ketoadipate catalyzed by E1alpha and beta (alpha ketoglutarate dehydrogenase). Lipoamide cofactor associated with E1 is reduced at the same time. Next, the glutaryl group derived from alpha ketoglutarate is transferred to coenzyme A in two steps catalyzed E2 (dihydrolipolyl transacetylase). Finally, the oxidized form of lipoamide is regenerated and electrons are transferred to NAD+ in two steps catalyzed by E3 (dihydrolipoyl dehydrogenase). The biochemical details of this reaction have been worked out with alpha ketoglutarate dehydrogenase complex and subunits purified from bovine tissue (McCartney et al. 1998). While all of the human proteins are known as predicted protein products of cloned genes, direct experimental evidence for their functions is available only for E3 (DLD) (Brautigam et al. 2005).
Identifier: R-HSA-5262606
Species: Homo sapiens
Compartment: cytosol
XAV939 binds to the catalytic sites of tankyrase 1 and 2 and inhibits the ADP-ribosylation of AXIN1 and 2. Treatment of cells with XAV939 significantly increases the protein, but not the mRNA levels of AXIN1 and 2 and supports a strong increase in the level of GSK3beta-AXIN complexes. These cells also show increased phosphorylation of beta-catenin, decreased beta-catenin protein levels and a corresponding decrease in beta-catenin dependent transcription. Treatment of DLD-1 cells with XAV939 has also been shown to inhibit proliferation (Huang et al, 2009). XAV939 has not been tested in a clinical setting.
Identifier: R-HSA-1299482
Species: Homo sapiens
Compartment: mitochondrial inner membrane
As inferred from the yeast TIM23 complex, the human TIMM23 complex resides in the inner membrane of the mitochondrion and transfers precursor proteins to the inner membrane. The presequences of proteins targeted to the inner membrane are transferred to the matrix where they are cleaved. Sequences in the mature regions of the proteins then interact with the TIMM23 complex to halt transfer across the inner membrane and the proteins are released laterally into the inner membrane. TIMM21 is required.
In yeast experimentally verified substrates of the TIM23 complex targeted to the inner membrane include CYB2, DLD (LDHD in human), ATP9 (ATP5G1 in human), COQ2, TIM54 (TIMM54 in human), COX4, COX5A, and ATP2 (ATP5B in human). Many other inner membrane proteins are believed to be substrates of the TIMM23 complex.

Interactor (1 results from a total of 1)

Identifier: P75393
Primary external reference: UniProt: P75393

Pathway (4 results from a total of 4)

Identifier: R-HSA-6783984
Species: Homo sapiens
The simplest amino acid, glycine, is catabolised by several different pathways. The major pathway is via the glycine cleavage system, comprising dimeric P protein (GLDC), T protein (AMT, GCST), dimeric L protein (DLD) and H protein (GCSH) (Kikuchi et al. 2008).
Identifier: R-HSA-5545619
Species: Homo sapiens
XAV939 binds to the catalytic sites of tankyrase 1 and 2 and inhibits the ADP-ribosylation of AXIN1 and 2. Treatment of cells with XAV939 significantly increases the protein, but not the mRNA levels of AXIN1 and 2 and supports a strong increase in the level of GSK3beta-AXIN complexes. These cells also show increased phosphorylation of beta-catenin, decreased beta-catenin protein levels and a corresponding decrease in beta-catenin dependent transcription. Treatment of DLD-1 cells with XAV939 has also been shown to inhibit proliferation (Huang et al, 2009). XAV939 has not been tested in a clinical setting.
Identifier: R-HSA-9853506
Species: Homo sapiens
Compartment: mitochondrial matrix
The mitochondrial alpha-oxoglutarate dehydrogenase complex (αOGDH, αKGDH, OGDHC) catalyzes the reaction of 2-oxoglutarate (2OG), CoASH, and NAD+ to form succinyl-CoA, CO2, and NADH. The enzyme complex ("metabolon") contains multiple copies of three different proteins, E1 (OGDH), E2 (DLST), and E3 (DLD), each with distinct catalytic activities (Reed and Hackert 1990; Zhou et al 2001). Specifically, it is composed of a core of 24 E2 subunits exhibiting octahedral symmetry. To these subunits are bound up to six E1 dimers and to each of these is bound an E3 dimer (Nagy et al., 2021; Skalidis et al., 2023) and to an adaptive MRPS36 unit (Hevler et al., 2023). The reaction starts with the oxidative decarboxylation of 2OG catalyzed by E1alpha and beta (alpha ketoglutarate dehydrogenase). Lipoamide cofactor associated with E2 is reduced at the same time. Next, the succinyl group derived from alpha ketoglutarate is transferred to coenzyme A in two steps catalyzed by E2 (dihydrolipolyl transacetylase). Finally, the oxidized form of lipoamide is regenerated and electrons are transferred to NAD+ in two steps catalyzed by E3 (dihydrolipoyl dehydrogenase). The biochemical details of this reaction have been worked out first with alpha ketoglutarate dehydrogenase complex and subunits purified from bovine tissue (McCartney et al. 1998).

Generation of reactive oxygen species by OGDHC is a major source of mitochondrial oxidative stress under certain pathological conditions.
Identifier: R-HSA-9861559
Species: Homo sapiens
Compartment: mitochondrial inner membrane, mitochondrial matrix
The mitochondrial pyruvate dehydrogenase complex catalyzes the reaction of pyruvate, CoASH, and NAD+ to form acetylCoA, CO2, and NADH. The enzyme complex contains multiple copies of E1 alpha, E1 beta, E2, and E3, each with distinct catalytic activities (Reed and Hackert 1990; Zhou et al 2001), and the X-component (PDHX) which is required for anchoring E3 to E2 (Hiromasa et al., 2004; Vijayakrishnan et al., 2010). The reaction starts with the oxidative decarboxylation of pyruvate catalyzed by E1 alpha and beta (pyruvate dehydrogenase). Lipoamide cofactor associated with E2 is reduced at the same time. Next, the acetyl group derived from pyruvate is transferred to coenzyme A in two steps catalyzed by E2 (DLAT, dihydrolipolyl transacetylase). Finally, the oxidized form of lipoamide is regenerated and electrons are transferred to NAD+ in two steps catalyzed by E3 (DLD, dihydrolipoyl dehydrogenase). The biochemical details of this reaction have been worked out with pyruvate dehydrogenase complex and subunits purified from bovine tissue and other non-human sources. Direct evidence for the roles of the corresponding human proteins comes from studies of patients expressing mutant forms of E1 alpha (Lissens et al. 2000), E1 beta (Brown et al. 2004), E2 (Head et al. 2005), and E3 (Brautigam et al. 2005). The most common PDH complex deficiencies are caused by defects in PDHA and PDHX but can be caused by defects in any component of the complex (e.g. Pavlu-Pereira et al., 2020; reviewed in Prasad et al., 2011).
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