Literature summary for 1.5.5.2 extracted from

Campbell, A.C.; Becker, D.F.; Gates, K.S.; Tanner, J.J.
Covalent modification of the flavin in proline dehydrogenase by thiazolidine-2-carboxylate (2020), ACS Chem. Biol., 15, 936-944 .

Search for more literature for 1.5.5.2

Crystallization (Commentary)

Crystallization (Comment)	Organism
inhibitor thiazolidine-2-carboxylate covalently binds to the N5 of the FAD in the PRODH domain. The modified FAD exhibits a large butterfly bend angle	Sinorhizobium meliloti

Inhibitors

Inhibitors	Comment	Organism	Structure
thiazolidine-2-carboxylate	a mechanism-based inactivator of PRODH. PRODH catalyzes the oxidation of thiazolidine-2-carboxylate at the C atom adjacent to the S atom of the thiazolidine ring (C5). Then, the N5 atom of the reduced FAD attacks the C5 of the oxidized T2C species, resulting in a covalent adduct	Sinorhizobium meliloti

Organism

Organism	UniProt	Comment	Textmining
Sinorhizobium meliloti	F7X6I3	bifunctional proline dehydrogenase/1-pyrroline-5-carboxylate dehydrogenase, cf. EC 1.2.1.88	-
Sinorhizobium meliloti SM11	F7X6I3	bifunctional proline dehydrogenase/1-pyrroline-5-carboxylate dehydrogenase, cf. EC 1.2.1.88	-

Synonyms

Synonyms	Comment	Organism
PRODH	-	Sinorhizobium meliloti
PutA	-	Sinorhizobium meliloti

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Release 2023.1 (January 2023)