Pyruvate dehydrogenase complex deficiency due to a point mutation (P188L) within the thiamine pyrophosphate binding loop of the E1 alpha subunit.
Hemalatha
S G
SG
Department of Biochemistry, Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA.
Kerr
D S
DS
Wexler
I D
ID
Lusk
M M
MM
Kaung
M
M
Du
Y
Y
Kolli
M
M
Schelper
R L
RL
Patel
M S
MS
D001483:Base Sequence; D001665:Binding Sites; D001706:Biopsy; D002478:Cells, Cultured; D018076:DNA, Complementary / Q000737:chemistry; D005347:Fibroblasts / Q000737:chemistry / Q000201:enzymology; D006801:Humans; D015151:Immunoblotting; D007223:Infant; D008297:Male; D008969:Molecular Sequence Data; D018482:Muscle, Skeletal / Q000737:chemistry / Q000201:enzymology; D009206:Myocardium / Q000737:chemistry / Q000201:enzymology; D017354:Point Mutation; D016133:Polymerase Chain Reaction; D011768:Pyruvate Dehydrogenase Complex / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D015325:Pyruvate Dehydrogenase Complex Deficiency Disease / Q000209:etiology / Q000235:genetics*; D012333:RNA, Messenger / Q000032:analysis; D017422:Sequence Analysis, DNA; D012867:Skin / Q000166:cytology; D013835:Thiamine Pyrophosphate / Q000378:metabolism*
D018076:DNA, Complementary; D011768:Pyruvate Dehydrogenase Complex; D012333:RNA, Messenger; D013835:Thiamine Pyrophosphate