Functional Versatility of the Human 2-Oxoadipate Dehydrogenase in the L-Lysine Degradation Pathway toward Its Non-Cognate Substrate 2-Oxopimelic Acid.
2-oxoadipate dehydrogenase
2-oxoadipate dehydrogenase complex
2-oxopimelate substrate
E1a promiscuity
H2O2 production
L-lysine degradation pathway
rare E1a variants
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
26 Jul 2022
26 Jul 2022
Historique:
received:
23
06
2022
revised:
23
07
2022
accepted:
24
07
2022
entrez:
28
7
2022
pubmed:
29
7
2022
medline:
30
7
2022
Statut:
epublish
Résumé
The human 2-oxoadipate dehydrogenase complex (OADHc) in L-lysine catabolism is involved in the oxidative decarboxylation of 2-oxoadipate (OA) to glutaryl-CoA and NADH (+H
Identifiants
pubmed: 35897808
pii: ijms23158213
doi: 10.3390/ijms23158213
pmc: PMC9367764
pii:
doi:
Substances chimiques
NAD
0U46U6E8UK
DHTKD1 protein, human
EC 1.2.4.2
Ketoglutarate Dehydrogenase Complex
EC 1.2.4.2
Lysine
K3Z4F929H6
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : NICHD NIH HHS
ID : R03 HD092878
Pays : United States
Organisme : NIH HHS
ID : GM050380, R15-GM116077
Pays : United States
Organisme : Hungarian Brain Research program 2
ID : 2017-1.2.1-NKP-2017-00002
Organisme : Semmelweis University
ID : STIA-OTKA-2021, TKP2021-EGA-25, TKP2021-EGA-25
Organisme : NICHD NIH HHS
ID : R21 HD088775
Pays : United States
Organisme : Eunice Kennedy Shriver National Institute of Child Health and Human Development
ID : R03HD092878, R21HD088775
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