Literature summary for 6.3.2.6 extracted from

Manjunath, K.; Jeyakanthan, J.; Sekar, K.
Catalytic pathway, substrate binding and stability in SAICAR synthetase: A structure and molecular dynamics study (2015), J. Struct. Biol., 191, 22-31.

Cloned(Commentary)

Cloned (Comment)	Organism
overexpression in Escherichia coli	Pyrococcus horikoshii

Crystallization (Commentary)

Crystallization (Comment)	Organism
co-crystallization of SAICAR synthetase from Pyrococcus horikoshii with substrates and other nucleotides produces eight ligand bound structures, five in C2221 and three in H3 space groups. These ligand bound complexes have minor structural deviations compared to their corresponding apo structures. In most of the structures the hydrolyzed product of the nucleotide triphosphates are bound to the enzyme	Pyrococcus horikoshii

Crystallization (Comment)

Organism

co-crystallization of SAICAR synthetase from Pyrococcus horikoshii with substrates and other nucleotides produces eight ligand bound structures, five in C2221 and three in H3 space groups. These ligand bound complexes have minor structural deviations compared to their corresponding apo structures. In most of the structures the hydrolyzed product of the nucleotide triphosphates are bound to the enzyme

Pyrococcus horikoshii

Organism

Organism	UniProt	Comment	Textmining
Pyrococcus horikoshii	O57978	-	-
Pyrococcus horikoshii OT-3	O57978	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Pyrococcus horikoshii

Synonyms

Synonyms	Comment	Organism
PH0239	locus name	Pyrococcus horikoshii
SAICAR synthetase	-	Pyrococcus horikoshii

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Release 2023.1 (January 2023)