Literature summary for 1.1.1.25 extracted from

Lee, H.H.
High-resolution structure of shikimate dehydrogenase from Thermotoga maritima reveals a tightly closed conformation (2012), Mol. Cells, 33, 229-233.

Crystallization (Commentary)

Crystallization (Comment)	Organism
determination of the crystal structure at 1.45 A by molecular replacement. The protein shows a monomeric architecture. The overall structure comprises the N-terminal alpha/beta sandwich domain for substrate binding and the C-terminal domain for NADP binding.the enzyme is in a tightly closed conf ormation, which should be open for catalysis. Four ammonium sulfate ions were identified in the structure. They are located in the active site and appear to mimic the role of the substrate in terms of the enzyme activity and stability	Thermotoga maritima

Crystallization (Comment)

Organism

determination of the crystal structure at 1.45 A by molecular replacement. The protein shows a monomeric architecture. The overall structure comprises the N-terminal alpha/beta sandwich domain for substrate binding and the C-terminal domain for NADP binding.the enzyme is in a tightly closed conf ormation, which should be open for catalysis. Four ammonium sulfate ions were identified in the structure. They are located in the active site and appear to mimic the role of the substrate in terms of the enzyme activity and stability

Thermotoga maritima

Organism

Organism	UniProt	Comment	Textmining
Thermotoga maritima	Q9WYI1	-	-
Thermotoga maritima ATCC 43589	Q9WYI1	-	-

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Release 2023.1 (January 2023)