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Information on EC 2.7.1.5 - rhamnulokinase and Organism(s) Escherichia coli and UniProt Accession P32171

for references in articles please use BRENDA:EC2.7.1.5
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Escherichia coli
UNIPROT: P32171 not found.
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
l-rhamnulose kinase, rhamnulose kinase, rhamnulokinase, l-rhamnulokinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L-rhamnulose kinase
-
kinase, rhamnulo-(phosphorylating)
-
-
-
-
L-rhamnulokinase
-
-
-
-
L-rhamnulose kinase
-
-
-
-
rhamnulose kinase
-
-
-
-
RhuK
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:L-rhamnulose 1-phosphotransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9030-52-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + L-fructose
ADP + L-fructose 1-phosphate
show the reaction diagram
-
-
-
?
ATP + L-rhamnulose
ADP + L-rhamnulose 1-phosphate
show the reaction diagram
-
-
-
?
ATP + D-psicose
ADP + D-psicose 1-phosphate
show the reaction diagram
-
-
-
?
ATP + D-ribulose
ADP + D-ribulose 1-phosphate
show the reaction diagram
-
-
-
?
ATP + D-sorbose
ADP + D-sorbose 1-phosphate
show the reaction diagram
-
-
-
?
ATP + L-fructose
ADP + L-fructose 1-phosphate
show the reaction diagram
-
-
-
?
ATP + L-fuculose
ADP + L-fuculose 1-phosphate
show the reaction diagram
-
-
-
?
ATP + L-rhamnulose
ADP + L-rhamnulose 1-phosphate
show the reaction diagram
ATP + L-tagatose
ADP + L-tagatose 1-phosphate
show the reaction diagram
-
-
-
?
ATP + L-xylulose
ADP + L-xylulose 1-phosphate
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + L-rhamnulose
ADP + L-rhamnulose 1-phosphate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
20
D-psicose
-
-
11
D-ribulose
-
-
26
D-sorbose
-
-
3
L-Fructose
-
-
3
L-Fuculose
-
-
0.2
L-rhamnulose
-
-
21
L-tagatose
-
-
1
L-xylulose
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
52000
gel filtration
54110
calculated from amino acid sequence
52000
-
x * 52000 + x * 54000, SDS-PAGE
54000
-
x * 52000 + x * 54000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 52000, gel filtration
?
-
x * 52000 + x * 54000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop and sitting drop vapour diffusion methods using 17% (w/v) PEG 8000 and 120 mM LiCl
the structure of the enzyme in a ternary complex with its substrates ADP and L-rhamnulose is determined at 1.55 A resolution. 0.209. The result is compared with the lower resolution structure of a corresponding complex containing L-fructose instead of L-rhamnulose. In light of the two established sugar positions and conformations, a number of rare sugars is modeled into the active center of L-rhamnulose kinase and the model structures are compared with the known enzymatic phosphorylation rates
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-mercaptoethanol
incubation over more than 5 h in fresh 20 mM 2-mercaptoethanol does not change the activity
dithiothreitol
incubation over more than 5 h in fresh 25 mM dithiothreitol does not change the activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE-Sepharose column chromatography and Superdex 200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli strain JM105
overexpression in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Badia, J.; Baldoma, L.; Aguilar, J.; Boronat, A.
Identification of the rhaA, rhaB and rhaD gene products from Escherichia coli K-12
FEMS Microbiol. Lett.
65
253-258
1989
Escherichia coli
Manually annotated by BRENDA team
Wilson, D.M.; Ajl, S.
Metabolism of L-rhamnose by Escherichia coli. II. The phosphorylation of L-rhamnulose
J. Bacteriol.
73
415-420
1957
Escherichia coli, Escherichia coli B / ATCC 11303
Manually annotated by BRENDA team
Fessner, W.D.; Badia, J.; Eyrisch, O.; Schneider, A.; Sinerius, G.
Enzymatic synthesis of rare ketose 1-phosphates
Tetrahedron Lett.
33
5231-5234
1992
Escherichia coli
-
Manually annotated by BRENDA team
Grueninger, D.; Schulz, G.E.
Structure and reaction mechanism of L-rhamnulose kinase from Escherichia coli
J. Mol. Biol.
359
787-797
2006
Escherichia coli (P32171), Escherichia coli
Manually annotated by BRENDA team
Grueninger, D.; Schulz, G.E.
Substrate spectrum of L-rhamnulose kinase related to models derived from two ternary complex structures
FEBS Lett.
581
3127-3130
2007
Escherichia coli (P32171), Escherichia coli
Manually annotated by BRENDA team