Search results for DLD

Showing 11 results out of 11

×

Species

Types

Compartments

Reaction types

Search properties

Species

Types

Compartments

Reaction types

Search properties

Protein (1 results from a total of 1)

DLD

Identifier: R-HSA-69978
Species: Homo sapiens
Compartment: mitochondrial matrix
Primary external reference: UniProt: DLD: P09622

Complex (1 results from a total of 1)

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

Reaction (6 results from a total of 6)

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-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-71401
Species: Homo sapiens
Compartment: mitochondrial matrix
The mitochondrial alpha-ketoglutarate dehydrogenase complex catalyzes the reaction of alpha-ketoglutarate, CoASH, and NAD+ to form succinyl-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 ketoglutarate catalyzed by E1alpha and beta (alpha ketoglutarate dehydrogenase). Lipoamide cofactor associated with E1 is reduced at the same time. Next, the succinyl 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-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-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.
Identifier: R-HSA-1299487
Species: Homo sapiens
Compartment: mitochondrial inner membrane, mitochondrial intermembrane space
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 TIMM23 complex appears to adopt different configurations (and perhaps different subunit compositions) depending on whether the substrate is destined for the inner membrane or the matrix. Here we refer to the TIMM23 SORT complex as the configuration that delivers inner membrane proteins. The TIMM21 subunit is required for this activity. In yeast, the N-terminal presequences of precursors first interact with TIM50 and TIM23 (TIMM50 and TIMM23 in human, Zhang et al. 2013). The TIM17 and TIM23 subunits (TIMM17 and TIMM23 in human) form a channel and are required to initiate translocation of precursors.
In yeast experimentally verified substrates of the TIM23 SORT 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 (2 results from a total of 2)

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.
Cite Us!