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Information on EC 2.8.1.8 - lipoyl synthase and Organism(s) Pseudomonas aeruginosa

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EC Tree
     2 Transferases
         2.8 Transferring sulfur-containing groups
             2.8.1 Sulfurtransferases
                2.8.1.8 lipoyl synthase
IUBMB 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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Pseudomonas aeruginosa
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Word Map
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  • 2.8.1.8
  • lipoylation
  • lipas
  • lipoic
  • iron-sulfur
  • octanoyl
  • 5\'-deoxyadenosyl
  • octanoyl-acp
  • octanoyltransferase
  • methylthiolation
  • 5'-radical
  • h-protein
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
hide
[protein]-N6-(octanoyl)-L-lysine
+
an [Fe-S] cluster scaffold protein carrying a [4Fe-4S]2+ cluster
+
2
S-adenosyl-L-methionine
+
2
oxidized [2Fe-2S] ferredoxin
+
6
H+
=
[protein]-N6-[(R)-dihydrolipoyl]-L-lysine
+
an [Fe-S] cluster scaffold protein
+
2
sulfide
+
4
Fe3+
+
2
L-methionine
+
2
5'-deoxyadenosine
+
2
reduced [2Fe-2S] ferredoxin
[protein]-N6-(octanoyl)-L-lysine
+
an [Fe-S] cluster scaffold protein carrying a [4Fe-4S]2+ cluster
+
2
+
2
+
6
=
[protein]-N6-[(R)-dihydrolipoyl]-L-lysine
+
an [Fe-S] cluster scaffold protein
+
2
+
4
+
2
+
2
+
2
Synonyms
lipoyl synthase, lipoate synthase, lips2, lip1p, tk2248, lipa protein, tk2109, lips1, more
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -
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 hide
189398-80-9
-
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A8G3QGK9_PSEAI
313
0
35335
TrEMBL
-
A0A2R3IPE7_PSEAI
323
0
36389
TrEMBL
-
A0A8G6GVV3_PSEAI
327
0
36705
TrEMBL
-
A0A8F9KGZ7_PSEAI
327
0
36791
TrEMBL
-
A0A8G7A5G0_PSEAI
327
0
36761
TrEMBL
-
A0A8G3I201_PSEAI
327
0
36715
TrEMBL
-
A0A367LWG9_PSEAI
118
0
13611
TrEMBL
-
A0A367LUW0_PSEAI
85
0
9309
TrEMBL
-
A0A0E3GPH6_PSEAI
323
0
36315
TrEMBL
-
A0A8G7PRM1_PSEAI
327
0
36763
TrEMBL
-
A0A8G8H4L5_PSEAI
327
0
36723
TrEMBL
-
A0A431XE03_PSEAI
327
0
36775
TrEMBL
-
A0A8G3PPE3_PSEAI
327
0
36703
TrEMBL
-
A0A069Q2Y9_PSEAI
327
0
36733
TrEMBL
-