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Information on EC 2.7.1.5 - rhamnulokinase for references in articles please use BRENDA:EC2.7.1.5
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EC Tree
The enzyme appears in viruses and cellular organisms
Synonyms
kinase, rhamnulo-(phosphorylating), L-rhamnulokinase, L-rhamnulose kinase, RhaB, rhamnulose kinase, RhuK,
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kinase, rhamnulo-(phosphorylating)
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rhamnulose kinase
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L-rhamnulose kinase
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RhuK
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ATP + L-rhamnulose = ADP + L-rhamnulose 1-phosphate
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phospho group transfer
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ATP:L-rhamnulose 1-phosphotransferase
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ATP + D-psicose
ADP + D-psicose 1-phosphate
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ATP + D-ribulose
ADP + D-ribulose 1-phosphate
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ATP + D-sorbose
ADP + D-sorbose 1-phosphate
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ATP + L-fructose
ADP + L-fructose 1-phosphate
ATP + L-fuculose
ADP + L-fuculose 1-phosphate
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ATP + L-fuculose
ADP + L-rhamnulose 1-phosphate
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81.3% of the activity with L-rhamnulose
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ATP + L-rhamnulose
ADP + L-rhamnulose 1-phosphate
ATP + L-tagatose
ADP + L-tagatose 1-phosphate
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ATP + L-xylulose
ADP + L-xylulose 1-phosphate
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additional information
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no substrates: L-rhamnose, L-fucose
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ATP + L-fructose
ADP + L-fructose 1-phosphate
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ATP + L-fructose
ADP + L-fructose 1-phosphate
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ATP + L-rhamnulose
ADP + L-rhamnulose 1-phosphate
Arthrobacter pyridinolis
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ATP + L-rhamnulose
ADP + L-rhamnulose 1-phosphate
Arthrobacter pyridinolis
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involved in metabolism of L-rhamnulose by a respiration-coupled transport system
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ATP + L-rhamnulose
ADP + L-rhamnulose 1-phosphate
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ATP + L-rhamnulose
ADP + L-rhamnulose 1-phosphate
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ATP + L-rhamnulose
ADP + L-rhamnulose 1-phosphate
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ATP + L-rhamnulose
ADP + L-rhamnulose 1-phosphate
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relatively broad tolerance for structural modifications of its natural substrate L-rhamnulose, requiring only absolute (3R)-stereochemistry for activity but allowing for inversion, (de)oxygenation or substitution at the remaining position
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ATP + L-rhamnulose
ADP + L-rhamnulose 1-phosphate
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ATP + L-rhamnulose
ADP + L-rhamnulose 1-phosphate
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ATP + L-rhamnulose
ADP + L-rhamnulose 1-phosphate
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ATP + L-rhamnulose
ADP + L-rhamnulose 1-phosphate
ATP + L-rhamnulose
ADP + L-rhamnulose 1-phosphate
Arthrobacter pyridinolis
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involved in metabolism of L-rhamnulose by a respiration-coupled transport system
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ATP + L-rhamnulose
ADP + L-rhamnulose 1-phosphate
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ATP + L-rhamnulose
ADP + L-rhamnulose 1-phosphate
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ATP + L-rhamnulose
ADP + L-rhamnulose 1-phosphate
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ATP + L-rhamnulose
ADP + L-rhamnulose 1-phosphate
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0.0047
Arthrobacter pyridinolis
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rhamnulosekinase activity in crude extract of strain SL23
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8.5
Arthrobacter pyridinolis
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assay at
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22
Arthrobacter pyridinolis
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assay at room temperature
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Arthrobacter pyridinolis
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brenda
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rhamnulokinase is induced by growth on L-rhamnose
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Uniprot
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K-12
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Escherichia coli (strain K12)
Escherichia coli (strain UTI89 / UPEC)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
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54000
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x * 52000 + x * 54000, SDS-PAGE
54110
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calculated from amino acid sequence
52000
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x * 52000 + x * 54000, SDS-PAGE
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?
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x * 52000 + x * 54000, SDS-PAGE
monomer
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1 * 52000, gel filtration
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hanging drop and sitting drop vapour diffusion methods using 17% (w/v) PEG 8000 and 120 mM LiCl
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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
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2-mercaptoethanol
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incubation over more than 5 h in fresh 20 mM 2-mercaptoethanol does not change the activity
dithiothreitol
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incubation over more than 5 h in fresh 25 mM dithiothreitol does not change the activity
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DEAE-Sepharose column chromatography and Superdex 200 gel filtration
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expressed in Escherichia coli strain JM105
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overexpression in Escherichia coli
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synthesis
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production of L-Rhamnulose (6-deoxy-L-arabino-2-hexulose) and L-fuculose (6-deoxy-L-lyxo-2-hexulose) from L-rhamnose and L-fucose. First, isomerization of L-rhamnose to L-rhamnulose, or L-fucose to L-fuculose is combined with a targeted phosphorylation reaction catalyzed by L-rhamnulose kinase (RhaB). The by-products (ATP and ADP) are selectively removed by silver nitrate precipitation method. In the second step, the phosphate group is hydrolyzed to produce L-rhamnulose or L-fuculose with purity exceeding 99% in more than 80% yield
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Levinson, S.L.; Krulwich, T.A.
Metabolism of L-rhamnose in Arthrobacter pyridinolis
J. Gen. Microbiol.
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277-286
1976
Arthrobacter pyridinolis
brenda
Akhy, M.T.; Brown, C.M.; Old, D.C.
L-Rhamnose utilization in Salmonella typhimurium
J. Appl. Bacteriol.
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269-274
1984
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
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.
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253-258
1989
Escherichia coli
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Wilson, D.M.; Ajl, S.
Metabolism of L-rhamnose by Escherichia coli. II. The phosphorylation of L-rhamnulose
J. Bacteriol.
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415-420
1957
Escherichia coli, Escherichia coli B / ATCC 11303
brenda
Fessner, W.D.; Badia, J.; Eyrisch, O.; Schneider, A.; Sinerius, G.
Enzymatic synthesis of rare ketose 1-phosphates
Tetrahedron Lett.
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5231-5234
1992
Escherichia coli
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Grueninger, D.; Schulz, G.E.
Structure and reaction mechanism of L-rhamnulose kinase from Escherichia coli
J. Mol. Biol.
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787-797
2006
Escherichia coli, Escherichia coli (P32171)
brenda
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, Escherichia coli (P32171)
brenda
Wen, L.; Zang, L.; Huang, K.; Li, S.; Wang, R.; Wang, P.
Efficient enzymatic synthesis of L-rhamnulose and L-fuculose
Bioorg. Med. Chem. Lett.
26
969-972
2016
Thermotoga maritima MSB8
brenda
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