Literature summary for 2.3.1.117 extracted from

Sagong, H.Y.; Kim, K.J.
Crystal structure and biochemical characterization of tetrahydrodipicolinate N-succinyltransferase from Corynebacterium glutamicum (2015), J. Agric. Food Chem., 63, 10641-10646.

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Corynebacterium glutamicum

Crystallization (Commentary)

Crystallization (Comment)	Organism
structure in complex with succinyl-CoA. Enzyme functions as a trimer, and each monomer consists of an N-terminal helical domain, a left-handed beta-helix domain, and a beta C-terminal domain. The position of the C-terminal domain changes slightly as the cofactor binds to the enzyme. The structure of DapD in complex with the substrate analogue 2-aminopimelate reveals that the analogue is stabilized by conserved residues	Corynebacterium glutamicum

Crystallization (Comment)

Organism

structure in complex with succinyl-CoA. Enzyme functions as a trimer, and each monomer consists of an N-terminal helical domain, a left-handed beta-helix domain, and a beta C-terminal domain. The position of the C-terminal domain changes slightly as the cofactor binds to the enzyme. The structure of DapD in complex with the substrate analogue 2-aminopimelate reveals that the analogue is stabilized by conserved residues

Corynebacterium glutamicum

Organism

Organism	UniProt	Comment	Textmining
Corynebacterium glutamicum	Q8NRE3	-	-
Corynebacterium glutamicum DSM 20300	Q8NRE3	-	-

Synonyms

Synonyms	Comment	Organism
DapD	-	Corynebacterium glutamicum

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Release 2023.1 (January 2023)