Information on EC 2.7.1.16 - ribulokinase

Substrates: -
Products: -

ATP + D-ribulose

ADP + D-ribulose 5-phosphate

Substrates: -
Products: -

ATP + D-ribulose

ADP + D-ribulose 5-phosphate

Substrates: phosphorylation at 25% the rate of L-isomer
Products: -

ATP + D-ribulose

ADP + D-ribulose 5-phosphate

Substrates: -
Products: -

ATP + D-ribulose

ADP + D-ribulose 5-phosphate

Substrates: phosphorylation at 25% the rate of L-isomer
Products: -

ATP + L-ribulose

ADP + L-ribulose 5-phosphate

Substrates: about 45% of the activity with D-ribulose
Products: -

ATP + L-ribulose

ADP + L-ribulose 5-phosphate

Substrates: about 45% of the activity with D-ribulose
Products: -

ATP + L-ribulose

ADP + L-ribulose 5-phosphate

Substrates: the enzyme is highly specific to L-ribulose
Products: -

ATP + L-ribulose

ADP + L-ribulose 5-phosphate

Substrates: -
Products: -

ATP + L-ribulose

ADP + L-ribulose 5-phosphate

Substrates: no substrates are both isomers of xylulose and other aldopentoses
Products: -

ATP + L-ribulose

ADP + L-ribulose 5-phosphate

Substrates: inducible enzyme of L-arabinose catabolism
Products: -

ATP + L-ribulose

ADP + L-ribulose 5-phosphate

Substrates: no substrates are both isomers of xylulose and other aldopentoses
Products: -

ATP + L-ribulose

ADP + L-ribulose 5-phosphate

Substrates: inducible enzyme of L-arabinose catabolism
Products: -

ATP + L-ribulose

ADP + L-ribulose 5-phosphate

Substrates: -
Products: -

ATP + L-ribulose

ADP + L-ribulose 5-phosphate

Halalkalibacterium halodurans

Substrates: the enzyme can recognize both L- and D-configurations of ribulose and catalyze phosphate addition to C5 with comparable kcat values
Products: -

ATP + L-ribulose

ADP + L-ribulose 5-phosphate

Substrates: ADP or UTP
Products: -

ATP + L-ribulose

ADP + L-ribulose 5-phosphate

Substrates: inducible enzyme of L-arabinose catabolism
Products: -

ATP + L-ribulose

ADP + L-ribulose 5-phosphate

Substrates: -
Products: -

ATP + L-ribulose

ADP + L-ribulose 5-phosphate

Substrates: -
Products: -

D-xylulose + ATP

D-xylose 5-phosphate + ADP

Substrates: -
Products: -

D-xylulose + ATP

D-xylose 5-phosphate + ADP

Substrates: -
Products: -

D-xylulose + ATP

D-xylulose 5-phosphate + ADP

Substrates: about 20% of the activity with D-ribulose
Products: -

D-xylulose + ATP

D-xylulose 5-phosphate + ADP

Substrates: about 20% of the activity with D-ribulose
Products: -

L-arabitol + ATP

L-arabitol 5-phosphate + ADP

Substrates: -
Products: -

L-arabitol + ATP

L-arabitol 5-phosphate + ADP

Substrates: -
Products: -

L-xylulose + ATP

L-xylose 5-phosphate + ADP

Substrates: -
Products: -

L-xylulose + ATP

L-xylose 5-phosphate + ADP

Substrates: -
Products: -

L-xylulose + ATP

L-xylulose 5-phosphate + ADP

Substrates: about 20% of the activity with D-ribulose
Products: -

L-xylulose + ATP

L-xylulose 5-phosphate + ADP

Substrates: about 20% of the activity with D-ribulose
Products: -

show all columns Go to Natural Substrate Search

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NATURAL SUBSTRATE

NATURAL PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

LITERATURE

COMMENTARY

REVERSIBILITY
r=reversible
ir=irreversible
?=not specified

ATP + D-ribulose

ADP + D-ribulose 5-phosphate

5 entries

ATP + L-ribulose

ADP + L-ribulose 5-phosphate

7 entries

ATP + D-ribulose

ADP + D-ribulose 5-phosphate

641010, 641013

Substrates: -
Products: -

ATP + D-ribulose

ADP + D-ribulose 5-phosphate

641010, 641013

Substrates: -
Products: -

ATP + D-ribulose

ADP + D-ribulose 5-phosphate

Substrates: -
Products: -

ATP + D-ribulose

ADP + D-ribulose 5-phosphate

Substrates: -
Products: -

ATP + D-ribulose

ADP + D-ribulose 5-phosphate

Substrates: -
Products: -

ATP + L-ribulose

ADP + L-ribulose 5-phosphate

Substrates: -
Products: -

ATP + L-ribulose

ADP + L-ribulose 5-phosphate

Substrates: inducible enzyme of L-arabinose catabolism
Products: -

ATP + L-ribulose

ADP + L-ribulose 5-phosphate

Substrates: inducible enzyme of L-arabinose catabolism
Products: -

ATP + L-ribulose

ADP + L-ribulose 5-phosphate

Substrates: -
Products: -

ATP + L-ribulose

ADP + L-ribulose 5-phosphate

Substrates: inducible enzyme of L-arabinose catabolism
Products: -

ATP + L-ribulose

ADP + L-ribulose 5-phosphate

Substrates: -
Products: -

ATP + L-ribulose

ADP + L-ribulose 5-phosphate

Substrates: -
Products: -

show all columns Go to Metals and Ions Search

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METALS and IONS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

Mg2+

4 entries

Mg2+

1 mM, increases ribulokinase activity up to 633%

Mg2+

requirement, Km-value: 1.3 mM

Mg2+

Mg2+

show all columns Go to Inhibitor Search

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INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

beta,gamma-imidoadenosine 5'-triphosphate

competitive inhibition to MgATP2- and uncompetitive to L-ribulose

L-erythrulose

p-chloromercuribenzoate

additional information

not inhibitory or activating: K+,Li+, Ca2+, and EDTA

L-erythrulose

competitive inhibition to L-ribulose

L-erythrulose

Halalkalibacterium halodurans

competitive inhibition

show all columns Go to Activating Compound Search

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ACTIVATING COMPOUND

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

2-mercaptoethanol

20 mM, increases ribulokinase activity up to 175%

show all columns Go to KM Value Search

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KM VALUE [mM]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.02 - 7

ATP

5 entries

5.5

D-ribitol

22°C, pH 7.5

0.27 - 0.94

D-ribulose

D-xylulose

22°C, pH 7.5

L-arabitol

22°C, pH 7.5

0.111 - 0.96

L-ribulose

3 entries

3.4

L-xylulose

22°C, pH 7.5

0.02

ATP

22°C, pH 7.5, L-ribulose

0.027

ATP

22°C, pH 7.5, D-ribulose or L-xylulose

0.076

ATP

37°C, pH 7.6

0.3 - 0.5

ATP

22°C, pH 7.5, D-xylulose, D-ribitol or L-arabitol

ATP

22°C, pH 7.5, without any sugar

0.27

D-ribulose

37°C, pH 7.6

0.39

D-ribulose

22°C, pH 7.5

0.94

D-ribulose

pH 9.0, 60°C

0.111

L-ribulose

37°C, pH 7.6

0.14

L-ribulose

22°C, pH 7.5

0.96

L-ribulose

in 50 mM Tris buffer (pH 7.5), at 30°C

show all columns Go to Turnover Number Search

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TURNOVER NUMBER [1/s]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.84

ATP

22°C, pH 7.5, without any sugar

109

D-ribitol

22°C, pH 7.5

D-ribulose

22°C, pH 7.5

D-xylulose

22°C, pH 7.5

L-arabitol

22°C, pH 7.5

41 - 80

L-ribulose

L-xylulose

22°C, pH 7.5

L-ribulose

show all columns Go to Specific Activity Search

in 50 mM Tris buffer (pH 7.5), at 30°C

L-ribulose

22°C, pH 7.5

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SPECIFIC ACTIVITY [µmol/min/mg]

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

11.6

show all columns Go to pH Optimum Search

833

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pH OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

show all columns Go to pH Range Search

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pH RANGE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

5 - 10

6 - 7.7

about half-maximal activity at pH 6 and pH 7.7

show all columns Go to Temperature Optimum Search

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TEMPERATURE OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

room temperature, assay at

assay at

assay at

show all columns Go to Temperature Range Search

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TEMPERATURE RANGE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

50 - 75

show all columns Go to Organism Search

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks include all textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks + FRENDAco-occurrence of enzyme names and organism names (less precise)

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ORGANISM

COMMENTARY

LITERATURE

UNIPROT

SEQUENCE DB

SOURCE

UniProt

brenda

UniProt

brenda

brenda

mutant araA-2

641010, 641013

brenda

Halalkalibacterium halodurans

UniProt

brenda

brenda

brenda

show all columns Go to Localization Search

brenda

brenda

mutant araA-2

brenda

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks

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LOCALIZATION

ORGANISM

UNIPROT

COMMENTARY

GeneOntology No.

LITERATURE

SOURCE

brenda

5829

brenda

top hide

Highest Expressing Human Cell Lines

Filter by:

Cell Line Links

Gene Links

show all columns Go to General Information Search

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GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

malfunction

inactivation of the araK gene severely impairs the growth on arabinose

Go to AA Sequence and Transmembrane Helices SearchGo to Localization Prediction

Show AA Sequence and Transmembrane Helices (6842 entries)
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.

Go to PDB and Structure Links Search

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PDB

SCOP

CATH

UNIPROT

ORGANISM

3qdk, download, 3D-view

SCOPe (3qdk)

CATH (3qdk)

Alkalihalobacillus halodurans

show all columns Go to Molecular Weight Search

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MOLECULAR WEIGHT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

61000

x * 61000, SDS-PAGE

96500 - 100000

osmotic pressure measurement, ultracentrifugation, ultracentrifugation and diffusion method

show all columns Go to Subunit Search

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SUBUNIT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

x * 61000, SDS-PAGE

x * 61000, SDS-PAGE

Go to Crystallization (commentary) Search

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

in complex with L-ribulose, vapor diffusion method, using 30% (w/v) PEG4000, 0.2 M sodium acetate, 0.1 M Tris, pH 8.5

Halalkalibacterium halodurans

show all columns Go to pH Stability Search

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pH STABILITY

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

30 min, 70% residual activity

739743

unstable below

641011

7.6

and above, stable at least 30 min at 60.5°C

641010

show all columns Go to Temperature Stability Search

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TEMPERATURE STABILITY

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

30 min, at least 90% residual activity

60.5

at least 30 min stable at pH 7.6

Go to General Stability Search

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GENERAL STABILITY

ORGANISM

UNIPROT

LITERATURE

dilute enzyme solutions are highly unstable

GSH stabilizes, but does not reactivate

Go to Storage Stability Search

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STORAGE STABILITY

ORGANISM

UNIPROT

LITERATURE

deeply frozen, several months

Go to Purification (commentary) Search

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PURIFICATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

3 entries

Ni-NTA affinity column chromatography

partial

Halalkalibacterium halodurans

Go to Cloned (commentary) Search

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CLONED (Commentary)

ORGANISM

UNIPROT

LITERATURE

expressed in Escherichia coli

expressed in Escherichia coli BL21(DE3)-codon+RIL cells

Halalkalibacterium halodurans

expression in Corynebacterium glutamicum. Corynebacterium glutamicum is metabolically engineered to broaden its substrate utilization range to include L-arabinose. The resultant CRA1 recombinant strain expressed the Escherichia coli genes araA, araB, and araD encoding L-arabinose isomerase, L-ribulokinase, and L-ribulose-5-phosphate 4-epimerase, respectively, under the control of a constitutive promoter. Unlike the wild-type strain, CRA1 is able to grow on mineral salts medium containing L-arabinose as the sole carbon and energy source. The three cloned genes are expressed to the same levels whether cells are cultured in the presence of D-glucose or L-arabinose. Strain CRA1 is able to utilize L-arabinose as a substrate for organic acid production even in the presence of D-glucose

671568

expression in Escherichia coli

expression in Saccharomyces cerevisiae. Improvement of a bacterial L-arabinose utilization pathway consisting of L-arabinose isomerase from Bacillus subtilis and L-ribulokinase and L-ribulose-5-phosphate 4-epimerase from Escherichia coli after expression of the corresponding genes in Saccharomyces cerevisiae. These improvements make up a new starting point for the construction of more-efficient industrial L-arabinose-fermenting yeast strains by evolutionary engineering

684574

show all columns Go to Application Search

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APPLICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

biotechnology

top print hide References Search

improvement of a bacterial L-arabinose utilization pathway consisting of L-arabinose isomerase from Bacillus subtilis and L-ribulokinase and L-ribulose-5-phosphate 4-epimerase from Escherichia coli after expression of the corresponding genes in Saccharomyces cerevisiae. These improvements make up a new starting point for the construction of more-efficient industrial L-arabinose-fermenting yeast strains by evolutionary engineering

684574

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REF.

AUTHORS

TITLE

JOURNAL

VOL.

PAGES

YEAR

ORGANISM (UNIPROT)

PUBMED ID

SOURCE

Lee, N.; Bendet, I.

Crystalline L-ribulokinase from Escherichia coli

J. Biol. Chem.

242

2043-2050

1967

Escherichia coli, Escherichia coli bB/r

5336963

brenda

Burman, D.P.; Horecker, B.L.

Pentose fermentation by Lactobacillus plantarum. III. Ribulokinase

J. Biol. Chem.

231

1039-1051

1958

Lactiplantibacillus plantarum, Lactiplantibacillus plantarum 124-2

13539035

brenda

Simpson, F.J.; Wood, W.A.

L-ribulose-5-phosphate: formation by purified kinase from Aerobacter aerogenes

J. Am. Chem. Soc.

5452-5453

1956

Klebsiella aerogenes

brenda

Lee, L.V.; Gerratana, B.; Cleland, W.W.

Substrate specificity and kinetic mechanism of Escherichia coli ribulokinase

Arch. Biochem. Biophys.

396

219-224

2001

Escherichia coli, Escherichia coli bB/r

11747300

brenda

671568

Kawaguchi, H.; Sasaki, M.; Vertes, A.A.; Inui, M.; Yukawa, H.

Engineering of an L-arabinose metabolic pathway in Corynebacterium glutamicum

Appl. Microbiol. Biotechnol.

1053-1062

2008

Escherichia coli

17965859

brenda

684574

Wiedemann, B.; Boles, E.

Codon-optimized bacterial genes improve L-arabinose fermentation in recombinant Saccharomyces cerevisiae

Appl. Environ. Microbiol.

2043-2050

2008

Escherichia coli

18263741

brenda

Zhang, L.; Leyn, S.A.; Gu, Y.; Jiang, W.; Rodionov, D.A.; Yang, C.

Ribulokinase and transcriptional regulation of arabinose metabolism in Clostridium acetobutylicum

J. Bacteriol.

194

1055-1064

2012

Clostridium acetobutylicum

22194461

brenda

Agarwal, R.; Burley, S.K.; Swaminathan, S.

Structural insight into mechanism and diverse substrate selection strategy of L-ribulokinase

Proteins

261-268

2012

Halalkalibacterium halodurans (Q9KBQ3)

22072612

brenda