Information on EC 2.7.1.5 - rhamnulokinase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.7.1.5
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RECOMMENDED NAME
GeneOntology No.
rhamnulokinase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + L-rhamnulose = ADP + L-rhamnulose 1-phosphate
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-rhamnose degradation I
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degradation of hexoses
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Pentose and glucuronate interconversions
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Fructose and mannose metabolism
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
ATP:L-rhamnulose 1-phosphotransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
9030-52-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Arthrobacter pyridinolis
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Manually annotated by BRENDA team
rhamnulokinase is induced by growth on L-rhamnose
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Manually annotated by BRENDA team
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-psicose
ADP + D-psicose 1-phosphate
show the reaction diagram
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?
ATP + D-ribulose
ADP + D-ribulose 1-phosphate
show the reaction diagram
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?
ATP + D-sorbose
ADP + D-sorbose 1-phosphate
show the reaction diagram
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-
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?
ATP + L-fructose
ADP + L-fructose 1-phosphate
show the reaction diagram
ATP + L-fuculose
ADP + L-fuculose 1-phosphate
show the reaction diagram
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?
ATP + L-rhamnulose
ADP + L-rhamnulose 1-phosphate
show the reaction diagram
ATP + L-tagatose
ADP + L-tagatose 1-phosphate
show the reaction diagram
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?
ATP + L-xylulose
ADP + L-xylulose 1-phosphate
show the reaction diagram
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?
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
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11
D-ribulose
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26
D-sorbose
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3
L-Fructose
0.2
L-rhamnulose
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21
L-tagatose
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1
L-xylulose
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0047
Arthrobacter pyridinolis
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rhamnulosekinase activity in crude extract of strain SL23
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5
Arthrobacter pyridinolis
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
Arthrobacter pyridinolis
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assay at room temperature
37
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assay at
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain UTI89 / UPEC)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
52000
gel filtration
54110
calculated from amino acid sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 52000, gel filtration
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
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