BCKDHB (P21953) deep research report (falcon / Edison Scientific Literature)
-
Frames the alpha2-beta2 E1 as a thiamine-diphosphate-dependent decarboxylase acting on all three branched-chain 2-oxo acids. This corroborated the ACCEPT calls on the IEA GO:0003863 and on the three granular Leu/Ile/Val catabolic-process terms, and informed the NEW thiamine pyrophosphate binding annotation.
"thiamine diphosphate (ThDP)-dependent decarboxylase"
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
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
Crystal structure of human branched-chain alpha-ketoacid dehydrogenase and the molecular basis of multienzyme complex deficiency in maple syrup urine disease.
Roles of His291-alpha and His146-beta' in the reductive acylation reaction catalyzed by human branched-chain alpha-ketoacid dehydrogenase: refined phosphorylation loop structure in the active site.
Cross-talk between thiamin diphosphate binding and phosphorylation loop conformation in human branched-chain alpha-keto acid decarboxylase/dehydrogenase.
Molecular mechanism for regulation of the human mitochondrial branched-chain alpha-ketoacid dehydrogenase complex by phosphorylation.
Maple syrup urine disease. Complete defect of the E1 beta subunit of the branched chain alpha-ketoacid dehydrogenase complex due to a deletion of an 11-bp repeat sequence which encodes a mitochondrial targeting leader peptide in a family with the disease.
Architecture of the human interactome defines protein communities and disease networks.
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.
Impaired assembly of E1 decarboxylase of the branched-chain alpha-ketoacid dehydrogenase complex in type IA maple syrup urine disease.
BCKDK phosphorylates BCKDH
PPM1K dephosphorylates p-BCKDH
BCKDHA:BCKDHB tetramer decarboxylates KIC, KMVA, KIV
DBT transfers BCAA to CoA
DLD dimer dehydrogenates dihydrolipoyl
DBT loss-of-function mutants don't synthesize BCAA-CoA
BCKDHA or BCKDHB loss-of-function mutants don't synthesize BCAA-CoA
Loss-of-function DLD mutants don't dehydrogenate dihydrolipoyl DBT
BCKDK loss-of-function mutations do not phosphorylate BCKDH
H139Hfs13* PPM1K does not dephosphorylate BCKDH