SIRT4 cleaves lipoyl from DLAT

Stable Identifier
R-HSA-9861626
Type
Reaction [transition]
Species
Homo sapiens
Compartment
mitochondrial matrix
ReviewStatus
5/5
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SIRT4 cleaves lipoyl from DLAT
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Mitochondrial NAD-dependent protein lipoamidase sirtuin-4 (SIRT4) hydrolyzes the lipoamide cofactors from the E2 component dihydrolipoyllysine acetyltransferase (DLAT) of the PDH complex, diminishing PDH activity. The reaction also irreversibly degrades one NAD+ molecule (Mathias et al., 2014). SIRT4 probably binds Zn2+ as a cofactor (UniProt).
Literature References
PubMed ID Title Journal Year
25525879 Sirtuin 4 is a lipoamidase regulating pyruvate dehydrogenase complex activity

Greco, TM, Shenk, T, Rowland, EA, Cristea, IM, Oberstein, A, Mathias, RA, Kang, Y, Budayeva, HG, Chakrabarti, R

Cell 2014
Participants
Input
Output
Participates
as an event of
Catalyst Activity

lipoamidase activity of SIRT4:Zn2+ [mitochondrial matrix]

Physical Entity
SIRT4:Zn2+ [mitochondrial matrix] (Homo sapiens)
Activity
lipoamidase activity (GO:0061690)
Orthologous Events
SIRT4 cleaves lipoyl from DLAT (Bos taurus)
SIRT4 cleaves lipoyl from DLAT (Caenorhabditis elegans)
SIRT4 cleaves lipoyl from DLAT (Canis familiaris)
SIRT4 cleaves lipoyl from DLAT (Danio rerio)
SIRT4 cleaves lipoyl from DLAT (Drosophila melanogaster)
SIRT4 cleaves lipoyl from DLAT (Gallus gallus)
SIRT4 cleaves lipoyl from DLAT (Mus musculus)
SIRT4 cleaves lipoyl from DLAT (Rattus norvegicus)
SIRT4 cleaves lipoyl from DLAT (Sus scrofa)
SIRT4 cleaves lipoyl from DLAT (Xenopus tropicalis)
Cross References
RHEA
Authored
Stephan, R  (2024-01-25)
Reviewed
Hill, DP  (2024-02-23)
Created
Stephan, R  (2024-02-21)
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