LAT1 (YNL071W, P12695) notes

Evidence journal for the review; sources are UniProt and cached publications.

• E2 (dihydrolipoyllysine-residue acetyltransferase, EC 2.3.1.12) of the PDH complex [UniProt:P12695].
• Activity of the catalytic domain: PMID:2271545; Asp-431 important for kcat.
• 60-mer core: PMID:9038189
• Reconstitution: PMID:7030741; PMID:7947791.
• E3 is recruited via protein X/Pdx1 PMID:2007123.

Curation decisions
- YeastPathways RCA 'is_active_in cytosol' (PYRUVDEHYD-PWY) was removed: the PDH complex is in the mitochondrial matrix. The same error appears on PDA1 and PDB1.
- Generic 'acyltransferase activity' and 'acetyltransferase complex' were changed to E2 activity / PDH complex.
- The YeastCyc reaction direction (acetyl-CoA + dihydrolipoyl-E2 <- ...) matches UniProt's RHEA:17017 written in reverse; physiologically acetyl transfer goes from the lipoyl arm to CoA.