Literature summary for 2.3.1.117 extracted from

Beaman, T.W.; Vogel, K.W.; Drueckhammer, D.G.; Blanchard, J.S.; Roderick, S.L.
Acyl group specificity at the active site of tetrahydrodipicolinate N-succinyltransferase (2002), Protein Sci., 11, 974-979.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure of the enzyme in ternary complexes with pimelate/succinyl-CoA and L-2-aminopimelate with the nonreactive cofactor analog succinamide-CoA, 2.3 and 2.0 A resolution, crystals are prepared by cocrystallization using the hanging drop vapor diffusion method, drops are formed by mixing 0.005 ml 27 mg/ml enzyme with an equal volume of 17% poly(ethylene glycol) 4000, 188 mM ammonium sulfate, 94 mM MES, pH 6.4, 4.7% 2-propanol, 20 mM pimelate, and 5 mM succinyl-CoA or 5 mM succinamide-CoA	Mycobacterium tuberculosis variant bovis

Crystallization (Comment)

Organism

crystal structure of the enzyme in ternary complexes with pimelate/succinyl-CoA and L-2-aminopimelate with the nonreactive cofactor analog succinamide-CoA, 2.3 and 2.0 A resolution, crystals are prepared by cocrystallization using the hanging drop vapor diffusion method, drops are formed by mixing 0.005 ml 27 mg/ml enzyme with an equal volume of 17% poly(ethylene glycol) 4000, 188 mM ammonium sulfate, 94 mM MES, pH 6.4, 4.7% 2-propanol, 20 mM pimelate, and 5 mM succinyl-CoA or 5 mM succinamide-CoA

Mycobacterium tuberculosis variant bovis

Organism

Organism	UniProt	Comment	Textmining
Mycobacterium tuberculosis variant bovis	-	-	-

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Release 2023.1 (January 2023)