Literature summary for 4.3.1.3 extracted from

Sanchez-Murcia, P.A.; Bueren-Calabuig, J.A.; Camacho-Artacho, M.; Cortes-Cabrera, A.; Gago, F.
Stepwise simulation of 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO) biogenesis in histidine ammonia-lyase (2016), Biochemistry, 55, 5854-5864 .

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Organism

Organism	UniProt	Comment	Textmining
Pseudomonas putida	P21310	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
additional information	a 3,5-dihydro-5-methylidene-4H-imidazol-4-one electrophilic moiety is post-translationally and autocatalytically generated in homotetrameric histidine ammonia-lyase containing the tripeptide Ala-Ser-Gly in a suitably positioned loop. Dehydration, rather than dehydrogenation by molecular oxygen, is the reaction that gives rise to the mature MIO ring system. Water molecules play a highly relevant role in the reaction mechanism. The backbone cyclization resulting from the nucleophilic attack of the Gly amide lone pair on the pi orbital of the Ala carbonyl precedes side-chain dehydration of the central serine	Pseudomonas putida

Subunits

Subunits	Comment	Organism
homotetramer	-	Pseudomonas putida

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Release 2023.1 (January 2023)