Literature summary for 2.7.1.4 extracted from

Nocek, B.; Stein, A.J.; Jedrzejczak, R.; Cuff, M.E.; Li, H.; Volkart, L.; Joachimiak, A.
Structural studies of ROK fructokinase YdhR from Bacillus subtilis: insights into substrate binding and fructose specificity (2011), J. Mol. Biol., 406, 325-342.

Search for more literature for 2.7.1.4

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli as a His-tagged fusion protein	Bacillus subtilis

Crystallization (Commentary)

Crystallization (Comment)	Organism
the crystal structures of ROK FK from Bacillus subtilis (a) apo and in the presence of (b) ADP and (c) ADP/D-fructose is shown. All structures show that YdhR is a homo-dimer with a monomer composed of two similar alpha/beta domains forming a large cleft between domains that bind ADP and D-fructose	Bacillus subtilis

Protein Variants

Protein Variants	Comment	Organism
G59A	point mutation of glycine 59 to alanine shows that this residue plays a critical role in specificity of YdhR to D-fructose. Point mutation nearly completely abolishes the fructokinase activity	Bacillus subtilis

Organism

Organism	UniProt	Comment	Textmining
Bacillus subtilis	O05510	-	-
Bacillus subtilis 168	O05510	-	-

Purification (Commentary)

Purification (Comment)	Organism
using Ni-NTA chromatography	Bacillus subtilis

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + D-fructose	-	Bacillus subtilis	ADP + D-fructose 6-phosphate	-	?
ATP + D-fructose	-	Bacillus subtilis 168	ADP + D-fructose 6-phosphate	-	?

Subunits

Subunits	Comment	Organism
homodimer	crystal structure	Bacillus subtilis

Synonyms

Synonyms	Comment	Organism
ROK FK	-	Bacillus subtilis
YdhR	-	Bacillus subtilis

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
25	-	assay at	Bacillus subtilis

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8	-	assay at	Bacillus subtilis

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Release 2023.1 (January 2023)