Literature summary for 2.3.1.94 extracted from

Argyropoulos, P.; Bergeret, F.; Pardin, C.; Reimer, J.M.; Pinto, A.; Boddy, C.N.; Schmeing, T.M.
Towards a characterization of the structural determinants of specificity in the macrocyclizing thioesterase for deoxyerythronolide B biosynthesis (2016), Biochim. Biophys. Acta, 1860, 486-497.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
structures of a construct of DEBS thioesterase domain alone at 1.7 A, and DEBS thioesterase domain bound with a simple allylphosphonate, prop-2-en-1-ylphosphonic acid, at 2.1 A resolution	Saccharopolyspora erythraea

Inhibitors

Inhibitors	Comment	Organism	Structure
(3R,5R)-diphenyl 6-(3,5-dihydroxy-6-phenylhexanoylamino)hexylphosphonate	phosphonate ester, close structural homolog of substrates known to undergo macrocyclization and hydrolysis. The ester effectively inhibits the enzyme, but does not lead to co-complex structures. Pretreatment of recombinant thioesterase, residues15-283, with inhibitor for 18 h abolishes enzymatic activity for hydrolysis of the N-acetyl-cysteamine thioester of 3-hydroxyheptanoate	Saccharopolyspora erythraea
(3S,5R)-diphenyl 6-(3,5-dihydroxy-6-phenylhexanoylamino)hexylphosphonate	phosphonate ester, close structural homolog of substrates known to undergo macrocyclization and hydrolysis. The ester effectively inhibits the enzyme, but does not lead to co-complex structures. Pretreatment of recombinant thioesterase, residues15-283, with inhibitor for 18 h abolishes enzymatic activity for hydrolysis of the N-acetyl-cysteamine thioester of 3-hydroxyheptanoate	Saccharopolyspora erythraea
prop-2-en-1-ylphosphonic acid	88% inhibition	Saccharopolyspora erythraea

Organism

Organism	UniProt	Comment	Textmining
Saccharopolyspora erythraea	Q03133	modules 5 and 6 including thioesterase domain	-

Synonyms

Synonyms	Comment	Organism
erythronolide synthase	-	Saccharopolyspora erythraea

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Release 2023.1 (January 2023)