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Literature summary for 4.1.1.72 extracted from

  • Wynn, R.M.; Ho, R.; Chuang, J.L.; Chuang, D.T.
    Roles of active site and novel K+ ion-binding site residues in human mitochondrial branched-chain alpha-ketoacid decarboxylase/dehydrogenase (2001), J. Biol. Chem., 276, 4168-4174.
    View publication on PubMed
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Application

Application Comment Organism
medicine in patients with maple syrup urine disease, mutations such as R114W-alpha or R220W-alpha cause a strongly reduced binding of thiamin diphosphate, rendering the enzyme inactive Homo sapiens

Protein Variants

Protein Variants Comment Organism
A240P-alpha slow assembly of alpha2beta2 tetramer Homo sapiens
E193A-alpha complete inactivation of enzyme Homo sapiens
E76A-beta’ complete inactivation of enzyme Homo sapiens
F364C-alpha slow assembly of enzyme, alphabeta dimer Homo sapiens
G204S-alpha slow assembly of alpha2beta2 tetramer Homo sapiens
G245R-alpha moderately slow assembly of alpha2beta2 tetramer Homo sapiens
H146A-beta’ complete inactivation of enzyme Homo sapiens
H291A-alpha partially active enzyme Homo sapiens
N222S-alpha markedly higher Km value for thiamin diphosphate Homo sapiens
R114W-alpha naturally occuring mutation in maple syrup disease patients, strongly reduced binding of thiamin diphosphate, enzyme inactive Homo sapiens
R220W-alpha naturally occuring mutation in maple syrup disease patients, strongly reduced binding of thiamin diphosphate, enzyme inactive Homo sapiens
T166M-alpha enzyme inactive, with attenuated ability to bind thiamin diphosphate Homo sapiens
T265R no assembly of alpha2beta2 tetramer Homo sapiens
Y224A-alpha markedly higher Km value for thiamin diphosphate Homo sapiens
Y368C-alpha slow assembly of enzyme as alphabeta dimer and alpha2beta2 tetramer Homo sapiens
Y393N-alpha slow assembly of enzyme, alphabeta dimer Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
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