Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.3.1.181 - lipoyl(octanoyl) transferase and Organism(s) Homo sapiens and UniProt Accession A6NK58

for references in articles please use BRENDA:EC2.3.1.181
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
This is the first committed step in the biosynthesis of lipoyl cofactor. Lipoylation is essential for the function of several key enzymes involved in oxidative metabolism, as it converts apoprotein into the biologically active holoprotein. Examples of such lipoylated proteins include pyruvate dehydrogenase (E2 domain), 2-oxoglutarate dehydrogenase (E2 domain), the branched-chain 2-oxoacid dehydrogenases and the glycine cleavage system (H protein) [2,3]. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the true substrate . The other enzyme involved in the biosynthesis of lipoyl cofactor is EC 2.8.1.8, lipoyl synthase. An alternative lipoylation pathway involves EC 6.3.1.20, lipoate---protein ligase, which can lipoylate apoproteins using exogenous lipoic acid (or its analogues).
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: A6NK58
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
lipoyltransferase, lipt2, lipb octanoyltransferase, lipoyl(octanoyl) transferase 2, atlip2p2, lip2p2, lipoyl(octanoyl) transferase, octanoyltransferase lipm, lipoyl (octanoyl)-acyl carrier protein:protein transferase, octanoyl (lipoyl) n-octanoyl (lipoyl) transferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
lipoyl(octanoyl) transferase 2
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
octanoyl-[acyl-carrier protein]:protein N-octanoyltransferase
This is the first committed step in the biosynthesis of lipoyl cofactor. Lipoylation is essential for the function of several key enzymes involved in oxidative metabolism, as it converts apoprotein into the biologically active holoprotein. Examples of such lipoylated proteins include pyruvate dehydrogenase (E2 domain), 2-oxoglutarate dehydrogenase (E2 domain), the branched-chain 2-oxoacid dehydrogenases and the glycine cleavage system (H protein) [2,3]. Lipoyl-ACP can also act as a substrate [4] although octanoyl-ACP is likely to be the true substrate [6]. The other enzyme involved in the biosynthesis of lipoyl cofactor is EC 2.8.1.8, lipoyl synthase. An alternative lipoylation pathway involves EC 6.3.1.20, lipoate---protein ligase, which can lipoylate apoproteins using exogenous lipoic acid (or its analogues).
CAS REGISTRY NUMBER
COMMENTARY hide
392687-64-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LIPT2_HUMAN
231
0
25195
Swiss-Prot
Mitochondrion (Reliability: 2)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Habarou, F.; Hamel, Y.; Haack, T.; Feichtinger, R.; Lebigot, E.; Marquardt, I.; Busiah, K.; Laroche, C.; Madrange, M.; Grisel, C.; Pontoizeau, C.; Eisermann, M.; Boutron, A.; Chrtien, D.; Chadefaux-Vekemans, B.; Barouki, R.; Bole-Feysot, C.; Nitschke, P
Biallelic mutations in LIPT2 cause a mitochondrial lipoylation defect associated with severe neonatal encephalopathy
Am. J. Hum. Genet.
101
283-290
2017
Homo sapiens (A6NK58)
Manually annotated by BRENDA team
Bernardinelli, E.; Costa, R.; Scantamburlo, G.; To, J.; Morabito, R.; Nofziger, C.; Doerrier, C.; Krumschnabel, G.; Paulmichl, M.; Dossena, S.
Mis-targeting of the mitochondrial protein LIPT2 leads to apoptotic cell death
PLoS ONE
12
e0179591
2017
Homo sapiens (A6NK58), Homo sapiens
Manually annotated by BRENDA team