Reactome | DLAT trimer transfers acetyl to CoA

DLAT trimer transfers acetyl to CoA

Stable Identifier

R-HSA-9861667

Type

Reaction [transition]

Species

Homo sapiens

Compartment

mitochondrial inner membrane, mitochondrial matrix

ReviewStatus

5/5

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Dihydrolipoyllysine-residue acetyltransferase (DLAT, PDHE2), the E2 component of the pyruvate dehydrogenase complex (PDC, PDHC), transfers the acetyl group from its acetyllipoyl-lysine residue onto coenzyme A (CoA) (Yang et al., 1997). Patients with primary biliary cirrhosis show autoantibodies against DLAT (Coppel et al., 1988). Defects in DLAT can cause PDH complex deficiency (PDHE2 deficiency, MIM:245348; Head et al., 2005)

Literature References

PubMed ID	Title	Journal	Year
16049940	Clinical and genetic spectrum of pyruvate dehydrogenase deficiency: dihydrolipoamide acetyltransferase (E2) deficiency Zolkipli, Z, Shahdadpuri, R, Head, RA, Brown, GK, Clayton, PT, King, MD, Brown, RM	Ann Neurol	2005
9045657	Assembly and full functionality of recombinantly expressed dihydrolipoyl acetyltransferase component of the human pyruvate dehydrogenase complex Song, J, Yang, D, Wagenknecht, T, Roche, TE	J Biol Chem	1997
3174635	Primary structure of the human M2 mitochondrial autoantigen of primary biliary cirrhosis: dihydrolipoamide acetyltransferase Surh, CD, Whittingham, S, Spithill, TW, Coppel, RL, Van de Water, J, McNeilage, LJ, Gershwin, ME	Proc Natl Acad Sci U S A	1988