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Information on EC 2.8.1.8 - lipoyl synthase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9ZWT1
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2.8.1.8 lipoyl synthaseIUBMB Comments
This enzyme catalyses the final step in the de-novo biosynthesis of the lipoyl cofactor, the attachment of two sulfhydryl groups to C6 and C8 of a pendant octanoyl chain. It is a member of the 'AdoMet radical' (radical SAM) family, all members of which produce the 5'-deoxyadenosin-5'-yl radical and methionine from AdoMet (S-adenosylmethionine) by the addition of an electron from an iron-sulfur centre. The enzyme contains two [4Fe-4S] clusters. The first cluster produces the radicals, which are converted into 5'-deoxyadenosine when they abstract hydrogen atoms from C6 and C8, respectively, leaving reactive radicals at these positions that interact with sulfur atoms within the second (auxiliary) cluster. Having donated two sulfur atoms, the auxiliary cluster is degraded during catalysis, but is regenerated immediately by the transfer of a new cluster from iron-sulfur cluster carrier proteins . 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) [1,2]. An alternative lipoylation pathway involves EC 6.3.1.20, lipoate---protein ligase, which can lipoylate apoproteins using exogenous lipoic acid (or its analogues) .
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Word Map
- 2.8.1.8
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lipoylation
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lipas
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lipoic
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iron-sulfur
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octanoyl
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5\'-deoxyadenosyl
- octanoyl-acp
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octanoyltransferase
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methylthiolation
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5'-radical
- h-protein
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
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2
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2
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6
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2
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4
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2
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[protein]-N6-(octanoyl)-L-lysine
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an [Fe-S] cluster scaffold protein carrying a [4Fe-4S]2+ cluster
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2
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2
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6
=
[protein]-N6-[(R)-dihydrolipoyl]-L-lysine
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an [Fe-S] cluster scaffold protein
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2
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4
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2
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2
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2
Synonyms
lipoyl synthase, lipoate synthase, lips2, lip1p, tk2248, lipa protein, tk2109, lips1, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
[protein]-N6-(octanoyl)-L-lysine:an [Fe-S] cluster scaffold protein carrying a [4Fe-4S]2+ cluster sulfurtransferase
This enzyme catalyses the final step in the de-novo biosynthesis of the lipoyl cofactor, the attachment of two sulfhydryl groups to C6 and C8 of a pendant octanoyl chain. It is a member of the 'AdoMet radical' (radical SAM) family, all members of which produce the 5'-deoxyadenosin-5'-yl radical and methionine from AdoMet (S-adenosylmethionine) by the addition of an electron from an iron-sulfur centre. The enzyme contains two [4Fe-4S] clusters. The first cluster produces the radicals, which are converted into 5'-deoxyadenosine when they abstract hydrogen atoms from C6 and C8, respectively, leaving reactive radicals at these positions that interact with sulfur atoms within the second (auxiliary) cluster. Having donated two sulfur atoms, the auxiliary cluster is degraded during catalysis, but is regenerated immediately by the transfer of a new cluster from iron-sulfur cluster carrier proteins [8]. 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) [1,2]. An alternative lipoylation pathway involves EC 6.3.1.20, lipoate---protein ligase, which can lipoylate apoproteins using exogenous lipoic acid (or its analogues) [4].
CAS REGISTRY NUMBER
COMMENTARY
189398-80-9
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
protein N6-(octanoyl)lysine + sulfur + S-adenosyl-L-methionine
protein N6-(lipoyl)lysine + L-methionine + 5'-deoxyadenosine
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-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
protein N6-(octanoyl)lysine + sulfur + S-adenosyl-L-methionine
protein N6-(lipoyl)lysine + L-methionine + 5'-deoxyadenosine
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-
-
?
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
the knockout of isoform LIP1p is fatal for early embryo development
physiological function
isoform LIP1 is indispensable for embryo development and essential for plastids
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). LIAS_ARATH
374
0
41344
Swiss-Prot
Mitochondrion (Reliability: 3)
REF.
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JOURNAL
VOL.
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ORGANISM (UNIPROT)
PUBMED ID
SOURCE
EXTERNAL LINKS (specific for EC-Number 2.8.1.8)
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