EC Number |
BRENDA No. |
Title |
Journal |
Volume |
Pages |
Year |
Organism |
PubMed ID |
---|
2.8.1.8 | 661727 |
Apicomplexan parasites contain a single lipoic acid synthase located in the plastid |
FEBS Lett. |
547 |
80-86 |
2003 |
Toxoplasma gondii |
12860390 |
2.8.1.8 | 661463 |
Assembly of the covalent linkage between lipoic acid and its cognate enzymes |
Chem. Biol. |
10 |
1293-1302 |
2003 |
Escherichia coli |
14700636 |
2.8.1.8 | 737720 |
Characterization of Lipoyl Synthase from Mycobacterium tuberculosis |
Biochemistry |
55 |
1372-1383 |
2016 |
Mycobacterium tuberculosis |
26841001 |
2.8.1.8 | 739557 |
Crystallographic snapshots of sulfur insertion by lipoyl synthase |
Proc. Natl. Acad. Sci. USA |
113 |
9446-9450 |
2016 |
Mycobacterium tuberculosis |
27506792 |
2.8.1.8 | 663290 |
Effect of iron-sulfur cluster assembly proteins on the expression of Escherichia coli lipoic acid synthase |
Protein Expr. Purif. |
28 |
241-245 |
2003 |
Escherichia coli |
12699687 |
2.8.1.8 | 661057 |
Escherichia coli LipA is a lipoyl synthase: in vitro biosynthesis of lipoylated pyruvate dehydrogenase complex from octanoyl-acyl carrier protein |
Biochemistry |
39 |
15166-15178 |
2000 |
Escherichia coli |
11106496 |
2.8.1.8 | 737696 |
Evidence for a catalytically and kinetically competent enzyme-substrate cross-linked intermediate in catalysis by lipoyl synthase |
Biochemistry |
53 |
4557-4572 |
2014 |
Escherichia coli |
24901788 |
2.8.1.8 | 737696 |
Evidence for a catalytically and kinetically competent enzyme-substrate cross-linked intermediate in catalysis by lipoyl synthase |
Biochemistry |
53 |
4557-4572 |
2014 |
Thermus thermophilus |
24901788 |
2.8.1.8 | 661982 |
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 |
J. Bacteriol. |
173 |
6411-6420 |
1991 |
Escherichia coli |
1655709 |
2.8.1.8 | 711217 |
Lipoic acid synthesis: a new family of octanoyltransferases generally annotated as lipoate protein ligases |
Biochemistry |
49 |
10024-10036 |
2010 |
Bacillus subtilis |
20882995 |