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Information on EC 2.7.1.4 - fructokinase and Organism(s) Bacillus subtilis and UniProt Accession O05510

for references in articles please use BRENDA:EC2.7.1.4
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Bacillus subtilis
UNIPROT: O05510 not found.
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The taxonomic range for the selected organisms is: Bacillus subtilis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
fk, fructokinase, mdfrk2, hore_18220, mdfrk1, putative fructokinase, vc-fk, atfrk6, atfrk7, d-fructokinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D-fructokinase
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D-fructose(D-mannose)kinase
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FK
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kinase, fructo- (phosphorylating)
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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SYSTEMATIC NAME
IUBMB Comments
ATP:D-fructose 6-phosphotransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
9030-51-7
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + D-fructose
ADP + D-fructose 6-phosphate
show the reaction diagram
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?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
crystal structure
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
using Ni-NTA chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli as a His-tagged fusion protein
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
J. Mol. Biol.
406
325-342
2011
Bacillus subtilis (O05510), Bacillus subtilis, Bacillus subtilis 168 (O05510)
Manually annotated by BRENDA team