Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Combined Automated Annotation using Multiple IEA Methods
Deep research on DLD function
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DLD is the L protein of the glycine cleavage system, reoxidising the dihydrolipoyl group on GCSH; corroborated by Reactome R-HSA-5694018
"In the GCS, DLD functions as the L-protein, catalyzing the final step of glycine degradation by reoxidizing the reduced lipoyl moiety on H-protein (GCSH)"
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Reports DLD among genes whose knockout blunts copper-induced (cuproptotic) cell death; a necessity result, not a GO-annotatable activity of DLD
"Genome-wide CRISPR screening identified DLD as one of seven genes"
Organization of the cores of the mammalian pyruvate dehydrogenase complex formed by E2 and E2 plus the E3-binding protein and their capacities to bind the E1 and E3 components.
A novel mutation in the dihydrolipoamide dehydrogenase E3 subunit gene (DLD) resulting in an atypical form of alpha-ketoglutarate dehydrogenase deficiency.
How dihydrolipoamide dehydrogenase-binding protein binds dihydrolipoamide dehydrogenase in the human pyruvate dehydrogenase complex.
Structural insight into interactions between dihydrolipoamide dehydrogenase (E3) and E3 binding protein of human pyruvate dehydrogenase complex.
Novel mutations in dihydrolipoamide dehydrogenase deficiency in two cousins with borderline-normal PDH complex activity.
Cryptic proteolytic activity of dihydrolipoamide dehydrogenase.
Subunit and catalytic component stoichiometries of an in vitro reconstituted human pyruvate dehydrogenase complex.
Interaction of E1 and E3 components with the core proteins of the human pyruvate dehydrogenase complex.
Characterization of interactions of dihydrolipoamide dehydrogenase with its binding protein in the human pyruvate dehydrogenase complex.
Phosphoproteome analysis of functional mitochondria isolated from resting human muscle reveals extensive phosphorylation of inner membrane protein complexes and enzymes.
Component co-expression and purification of recombinant human pyruvate dehydrogenase complex from baculovirus infected SF9 cells.
Architecture of the human interactome defines protein communities and disease networks.
A Map of Human Mitochondrial Protein Interactions Linked to Neurodegeneration Reveals New Mechanisms of Redox Homeostasis and NF-κB Signaling.
The mitochondrial 2-oxoadipate and 2-oxoglutarate dehydrogenase complexes share their E2 and E3 components for their function and both generate reactive oxygen species.
KAT2A coupled with the α-KGDH complex acts as a histone H3 succinyltransferase.
A reference map of the human binary protein interactome.
Cloning and cDNA sequence of the dihydrolipoamide dehydrogenase component human alpha-ketoacid dehydrogenase complexes.
Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.
Purification and characterization of human liver branched-chain alpha-keto acid dehydrogenase complex.
MRPS36 provides a structural link in the eukaryotic 2-oxoglutarate dehydrogenase complex.
Biochemical characterization of patients with dihydrolipoamide dehydrogenase deficiency.
Identification of two missense mutations in a dihydrolipoamide dehydrogenase-deficient patient.
Dihydrolipoamide dehydrogenase-binding protein of the human pyruvate dehydrogenase complex. DNA-derived amino acid sequence, expression, and reconstitution of the pyruvate dehydrogenase complex.
PDK isozymes phosphorylate PDHC subunit E1
PDP1,2 dephosphorylate p-lipo-PDH
BCKDK phosphorylates BCKDH
PPM1K dephosphorylates p-BCKDH
DLD dimer:2xFAD oxidises GCSH:DHLL to GCSH:lipoate
OGDH dimer decarboxylates 2-OG
CLPXP binds mitochondrial matrix proteins
CLPXP degrades mitochondrial matrix proteins
DLD dimer dehydrogenates dihydrolipoyl
DLST transfers succinyl to CoA
DHTKD1 dimer decarboxylates 2-OA
DLD dimer dehydrogenates dihydrolipoyl
DLST transfers glutaryl to CoA
BCKDHA:BCKDHB tetramer decarboxylates KIC, KMVA, KIV
DBT transfers BCAA to CoA
DLD dimer dehydrogenates dihydrolipoyl
DLD dimer dehydrogenates dihydrolipoyl
DLAT trimer transfers acetyl to CoA
PDH E1 decarboxylates PYR, transferring acetyl to DLAT
DBT loss-of-function mutants don't synthesize BCAA-CoA
BCKDK loss-of-function mutations do not phosphorylate BCKDH
H139Hfs13* PPM1K does not dephosphorylate BCKDH