Literature summary extracted from

Libreros-Zuniga, G.A.; Dos Santos Silva, C.; Salgado Ferreira, R.; Dias, M.V.B.
Structural basis for the interaction and processing of beta-lactam antibiotics by L,D-transpeptidase 3 (LdtMt3) from Mycobacterium tuberculosis (2019), ACS Infect. Dis., 5, 260-271 .

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
2.3.2.B14	apo and faropenem-acylated forms of Ldt3 at 1.3 and 1.8 A resolution, respectively. The structures revealed a fold and catalytic diad similar to those of other Ldt enzymes. Docking of beta-lactam antibiotics at the active site suggests interaction with conserved amino acids. Faropenem may be degraded after Cys246 acylation, and possibly only a beta-hydroxybutanoate or an acetyl group covalently attached to the enzyme remains	Mycobacterium tuberculosis

Organism

EC Number	Organism	UniProt	Comment	Textmining
2.3.2.B14	Mycobacterium tuberculosis	O06825	isoform L,D-transpeptidase 3	-
2.3.2.B14	Mycobacterium tuberculosis H37Rv	O06825	isoform L,D-transpeptidase 3	-

Synonyms

EC Number	Synonyms	Comment	Organism
2.3.2.B14	Rv1433	-	Mycobacterium tuberculosis

Temperature Stability [°C]

EC Number	Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
2.3.2.B14	additional information	-	in presence of beta-lactam antibiotics, a thermal shift ranging from -6.1°C for biapenem to 2.2°C for faropenem is observed	Mycobacterium tuberculosis
2.3.2.B14	40.9	-	melting temperature	Mycobacterium tuberculosis

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Release 2023.1 (January 2023)