Hydrolases;
Acting on carbon-sulfur bonds;
Thioether and trialkylsulfonium hydrolases
BRITE hierarchy

[protein]-(methyl)lanthionine hydrolase

(1) a [protein]-L-serine + a [protein]-L-cysteine = a [protein] with lanthionine crosslink + H2O (overall reaction) [RN:R13365];
(1a) a [protein]-L-serine = a [protein]-2-aminoprop-2-enoate + H2O [RN:R13366];
(1b) a [protein]-2-aminoprop-2-enoate + a [protein]-L-cysteine = a [protein] with lanthionine crosslink [RN:R13367];
(2) a [protein]-L-threonine + a [protein]-L-cysteine = a [protein] with 3-methyllanthionine crosslink + H2O (overall reaction) [RN:R13368];
(2a) a [protein]-L-threonine = a [protein]-(Z)-2-aminobutenoate + H2O [RN:R13369];
(2b) a [protein]-(Z)-2-aminobutenoate + a [protein]-L-cysteine = a [protein] with 3-methyllanthionine crosslink [RN:R13370]

R13365 R13366 R13367 R13368 R13369 R13370
Reaction

[protein]-L-serine [CPD:C02189];
[protein]-L-cysteine [CPD:C02743];
[protein]-2-aminoprop-2-enoate;
[protein]-L-threonine [CPD:C19803];
[protein]-(Z)-2-aminobutenoate [CPD:C22956]

The lanthipeptides are a family of ribosomally synthesized and post-translationally modified peptides (RiPPs) that is characterized by the presence of multiple lanthionine (Lan) and 3-methyllanthionine (MeLan) crosslinks, which are formed by lanthipeptide synthases. These enzymes catalyse dehydration of Ser/Thr residues, followed by intramolecular addition of the thiol group of a Cys residue to the dehydro amino acids, which results in the formation of the thioether crosslinks of (methyl)lanthionine.

EC 3.13.2.4 created 2024