Entry
Symbol
DHKTD1
Name
2-oxoadipate dehydrogenase E1 component [EC:1.2.4.-]
Pathway
map01110 Biosynthesis of secondary metabolites
map01210 2-Oxocarboxylic acid metabolism
Module
M00032 Lysine degradation, lysine => saccharopine => acetoacetyl-CoA
Disease
H00264 Charcot-Marie-Tooth disease
H02644 Alpha-aminoadipic and alpha-ketoadipic aciduria
Brite
KEGG Orthology (KO) [BR:ko00001 ]
09100 Metabolism
09105 Amino acid metabolism
00310 Lysine degradation
K15791 DHKTD1; 2-oxoadipate dehydrogenase E1 component
00380 Tryptophan metabolism
K15791 DHKTD1; 2-oxoadipate dehydrogenase E1 component
09108 Metabolism of cofactors and vitamins
00785 Lipoic acid metabolism
K15791 DHKTD1; 2-oxoadipate dehydrogenase E1 component
09180 Brite Hierarchies
09182 Protein families: genetic information processing
03029 Mitochondrial biogenesis
K15791 DHKTD1; 2-oxoadipate dehydrogenase E1 component
Enzymes [BR:ko01000 ]
1. Oxidoreductases
1.2 Acting on the aldehyde or oxo group of donors
1.2.4 With a disulfide as acceptor
1.2.4.-
K15791 DHKTD1; 2-oxoadipate dehydrogenase E1 component
Mitochondrial biogenesis [BR:ko03029 ]
Mitochondrial quality control factors
Regulator of mitochondrial biogenesis
Other regulator of mitochondrial biogenesis
K15791 DHKTD1; 2-oxoadipate dehydrogenase E1 component
BRITE hierarchy
Other DBs
Genes
» show all
Taxonomy UniProt
Reference
Authors
Xu W, Zhu H, Gu M, Luo Q, Ding J, Yao Y, Chen F, Wang Z
Title
DHTKD1 is essential for mitochondrial biogenesis and function maintenance.
Journal
Reference
Authors
Nagase T, Kikuno R, Nakayama M, Hirosawa M, Ohara O
Title
Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro.
Journal
Reference
Authors
Nemeria NS, Gerfen G, Nareddy PR, Yang L, Zhang X, Szostak M, Jordan F
Title
The mitochondrial 2-oxoadipate and 2-oxoglutarate dehydrogenase complexes share their E2 and E3 components for their function and both generate reactive oxygen species.
Journal
LinkDB
All DBs