Literature summary for 2.8.1.8 extracted from

Dong, G.; Cao, L.; Ryde, U.
Insight into the reaction mechanism of lipoyl synthase a QM/MM study (2018), J. Biol. Inorg. Chem., 23, 221-229 .

Search for more literature for 2.8.1.8

Organism

Organism	UniProt	Comment	Textmining
Mycobacterium tuberculosis	P9WK91	-	-
Mycobacterium tuberculosis ATCC 25618	P9WK91	-	-

Synonyms

Synonyms	Comment	Organism
LipA	-	Mycobacterium tuberculosis

Cofactor

Cofactor	Comment	Organism	Structure
[4Fe-4S]-center	the ground state of the two FeS clusters, both in the [4Fe4S]2+ oxidation state, is a singlet state with antiferromagnetically coupled high-spin Fe ions. There is a large variation of the energies of the various broken-symmetry states, up to 40 kJ/mol. For the two S-insertion reactions, the highest energy barrier is found for the hydrogen-atom abstraction from the octanoyl substrate by 5'-dA radical. The formation of 5'-dA radical shows an energy barrier of 6 kJ/mol for the first S-insertion reaction and no barrier for the second S-insertion reaction. Thehe first S ion attack on the C6 radical of octanoyl takes place directly by the transfer of the H6 from the substrate to 5'-dA radical, whereas for the second S-insertion reaction, a C8 radical intermediate is formed with a rate-limiting barrier of 71 kJ/mol	Mycobacterium tuberculosis

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)