Literature summary for 1.3.1.12 extracted from

Ku, H.K.; Do, N.H.; Song, J.S.; Choi, S.; Yeon, S.H.; Shin, M.H.; Kim, K.J.; Park, S.R.; Park, I.Y.; Kim, S.K.; Lee, S.J.
Crystal structure of prephenate dehydrogenase from Streptococcus mutans (2011), Int. J. Biol. Macromol., 49, 761-766.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Streptococcus mutans

Crystallization (Commentary)

Crystallization (Comment)	Organism
to 2.1 A resolution. The N-terminal alpha/beta domain has a Rossman fold for binding a NAD+ molecule. The C-terminal domain adopts a helical architecture and is involved in homo-dimerization. NAD+ binding stabilizes the active site and facilitates the substrate, prephenate, binding	Streptococcus mutans

Organism

Organism	UniProt	Comment	Textmining
Streptococcus mutans	Q8DUW0	-	-
Streptococcus mutans ATCC 700610	Q8DUW0	-	-

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Release 2023.1 (January 2023)