EC number:2.8.1.8
Enzyme
Download| EC Tree |
| 2. Transferases |
| 2.8 Transferring sulfur-containing groups |
| 2.8.1 Sulfurtransferases |
| ID: | 2.8.1.8 |
|---|---|
| Description: | Lipoyl synthase. |
| Alternative Name: |
Lipoate synthase. |
| Cath: | 3.30.930.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 2.8.1.8 |
| BRENDA Enzyme Link: | BRENDA 2.8.1.8 |
| KEGG Enzyme Link: | KEGG2.8.1.8 |
| BioCyc Enzyme Link: | BioCyc 2.8.1.8 |
| ExPASy Enzyme Link: | ExPASy2.8.1.8 |
| EC2PDB Enzyme Link: | EC2PDB 2.8.1.8 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.8.1.8 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.8.1.8 |
| IntEnz Enzyme Link: | IntEnz 2.8.1.8 |
| MEDLINE Enzyme Link: | MEDLINE 2.8.1.8 |
| RHEA:16585 | [[Fe-S] cluster scaffold protein carrying a second [4Fe-4S](2+) cluster] + 4 H(+) + N(6)-octanoyl-L-lysyl-[protein] + 2 oxidized [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + 2 5'-deoxyadenosine + [[Fe-S] cluster scaffold protein] + 4 Fe(3+) + 2 hydrogen sulfide + 2 L-methionine + 2 reduced [2Fe-2S]-[ferredoxin] |
| RULE(radius=1) | [*;H0;+0:1]-[SH;+0:2].[*;H0;+0:3]-[SH;+0:4].[*:5]-[CH2;+0:6]-[*:7]-[CH3;+0:8].[*:9]-[CH2;+0:10]-[S+;H0:11](-[*:12])-[*:13].[*:14]-[Fe;H0;+0:15]-[*:16].[*:17]-[Fe;H0;+0:18]-[*:19].[*:20]-[S+;H0:21](-[*:22])-[CH2;+0:23]-[*:24]>>[*;H0;+0:1].[*;H0;+0:3].[*:9]-[CH3;+0:10].[*:24]-[CH3;+0:23].[*:5]-[CH;+0:6]1-[*:7]-[CH2;+0:8]-[S;H0;+0:4]-[S;H0;+0:2]-1.[*:14]-[Fe+;H0:15]-[*:16].[*:17]-[Fe+;H0:18]-[*:19].[*:12]-[S;H0;+0:11]-[*:13].[*:20]-[S;H0;+0:21]-[*:22] |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| A new metabolic link. The acyl carrier protein of lipid synthesis donates lipoic acid to the pyruvate dehydrogenase complex in Escherichia coli and mitochondria. | Jordan SW, Cronan JE Jr | 1997 Jul 18 | 9218413 |
| Self-sacrifice in radical S-adenosylmethionine proteins. | Booker SJ, Cicchillo RM, Grove TL | 2007 Oct | 17936058 |
| Lipoic acid metabolism in Escherichia coli: isolation of null mutants defective in lipoic acid biosynthesis, molecular cloning and characterization of the E. coli lip locus, and identification of the lipoylated protein of the glycine cleavage system. | Vanden Boom TJ, Reed KE, Cronan JE Jr | 1991 Oct | 1655709 |
| Mechanistic investigations of lipoic acid biosynthesis in Escherichia coli: both sulfur atoms in lipoic acid are contributed by the same lipoyl synthase polypeptide. | Cicchillo RM, Booker SJ | 2005 Mar 9 | 15740115 |
| Lipoyl synthase requires two equivalents of S-adenosyl-L-methionine to synthesize one equivalent of lipoic acid. | Cicchillo RM, Iwig DF, Jones AD, Nesbitt NM, Baleanu-Gogonea C, Souder MG, Tu L, Booker SJ | 2004 Jun 1 | 15157071 |
| Assembly of the covalent linkage between lipoic acid and its cognate enzymes. | Zhao X, Miller JR, Jiang Y, Marletta MA, Cronan JE | 2003 Dec | 14700636 |
| Escherichia coli LipA is a lipoyl synthase: in vitro biosynthesis of lipoylated pyruvate dehydrogenase complex from octanoyl-acyl carrier protein. | Miller JR, Busby RW, Jordan SW, Cheek J, Henshaw TF, Ashley GW, Broderick JB, Cronan JE Jr, Marletta MA | 2000 Dec 12 | 11106496 |
| Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. | Perham RN | 2000 | 10966480 |
| Destruction and reformation of an iron-sulfur cluster during catalysis by lipoyl synthase. | McCarthy EL, Booker SJ | 2017 Oct 20 | 29051382 |