Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 5.4.2.7 - phosphopentomutase and Organism(s) Escherichia coli and UniProt Accession P0A6K6

for references in articles please use BRENDA:EC5.4.2.7
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     5 Isomerases
         5.4 Intramolecular transferases
             5.4.2 Phosphotransferases (phosphomutases)
                5.4.2.7 phosphopentomutase
IUBMB Comments
Also converts 2-deoxy-alpha-D-ribose 1-phosphate into 2-deoxy-D-ribose 5-phosphate. alpha-D-Ribose 1,5-bisphosphate, 2-deoxy-alpha-D-ribose 1,5-bisphosphate, or alpha-D-glucose 1,6-bisphosphate can act as cofactor.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Escherichia coli
UNIPROT: P0A6K6
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
phosphopentomutase, phosphoribomutase, phosphodeoxyribomutase, deoxyribomutase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphopentomutase
-
alpha-D-Glucose-1,6-bisphosphate:deoxy-D-ribose-1-phosphate phosphotransferase
-
-
-
-
Deoxyribomutase
-
-
-
-
Deoxyribose phosphomutase
-
-
-
-
Phosphodeoxyribomutase
-
-
-
-
Phosphomutase, deoxyribose
-
-
-
-
Phosphoribomutase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isomerization
-
isomerization
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
alpha-D-ribose 1,5-phosphomutase
Also converts 2-deoxy-alpha-D-ribose 1-phosphate into 2-deoxy-D-ribose 5-phosphate. alpha-D-Ribose 1,5-bisphosphate, 2-deoxy-alpha-D-ribose 1,5-bisphosphate, or alpha-D-glucose 1,6-bisphosphate can act as cofactor.
CAS REGISTRY NUMBER
COMMENTARY hide
9026-77-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-D-ribose 1-phosphate
D-ribose 5-phosphate
show the reaction diagram
-
-
-
?
2-deoxy-D-ribose 5-phosphate
2-deoxy-D-ribose 1-phosphate
show the reaction diagram
-
-
-
-
r
2-deoxyribose 5-phosphate
2-deoxyribose 1-phosphate
show the reaction diagram
2-Deoxyribose 5-phosphate
?
show the reaction diagram
-
-
-
-
?
alpha-D-arabinose 5-phosphate
alpha-D-arabinose 1-phosphate
show the reaction diagram
-
-
-
-
?
alpha-D-pentose 5-phosphate
alpha-D-pentose 1-phosphate
show the reaction diagram
-
-
-
-
?
alpha-D-ribose 1-phosphate
alpha-D-ribose 5-phosphate
show the reaction diagram
-
-
-
-
r
alpha-D-ribose 1-phosphate
D-ribose 5-phosphate
show the reaction diagram
-
-
-
-
?
D-Arabinose 5-phosphate
D-Arabinose 1-phosphate
show the reaction diagram
-
-
-
-
?
D-ribose 1-phosphate
D-ribose 5-phosphate
show the reaction diagram
Deoxyribose 1-phosphate
Deoxyribose 5-phosphate
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
does not accept 2,3-dideoxyribose 5-phosphate as substrate
-
-
?
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
alpha-D-ribose 1-phosphate
D-ribose 5-phosphate
show the reaction diagram
-
-
-
?
2-Deoxyribose 5-phosphate
?
show the reaction diagram
-
-
-
-
?
alpha-D-ribose 1-phosphate
D-ribose 5-phosphate
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
activity is dependent on Mn2+, Ni2+ or Co2+. Optimal concentration: 0.05-0.06 mM
Ni2+
-
activity is dependent on Mn2+, Ni2+ or Co2+. Optimal concentration: 0.05 mM with deoxyribose 1-phosphate and 0.09 mM with ribose 1-phosphate as substrate
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
-
in presence of 0.2 mM CoCl2
Cd2+
-
in presence of 0.2 mM CoCl2
Cu2+
-
in presence of 0.2 mM CoCl2
Fe3+
-
in presence of 0.2 mM CoCl2
phosphate
-
50 mM, 95% inhibition
SO42-
-
50 mM, 85% inhibition
Zn2+
-
in presence of 0.2 mM CoCl2
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
alpha-D-Glucose 1,6-bisphosphate
-
about 7fold increase of activity at 0.001 mM
D-glucose 1,6-diphosphate
-
-
Deoxyribose-1,5-diphosphate
-
10fold stimulation, Km: 0.00017 mM, optimal concentration: 0.0014 mM
glucose 1,6-diphosphate
-
3fold stimulation, Km: 0.00008 mM, optimal concentration: 0.0007 mM
ribose-1,5-diphosphate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.013 - 0.022
deoxyribose 1-phosphate
0.043
ribose 1-phosphate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
46000
determined by SDS-PAGE
32000
-
gel filtration
43000
-
1 * 43000, enzyme form I, II and III, SDS-PAGE
45000
-
equilibrium centrifugation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 43000, SDS-PAGE
monomer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
half-life of the cobalt-enzyme in 1 mM EDTA: 15 min for enzyme form I, 31 min for enzyme form II
50
-
enzyme immobilized on CNBr-Ag is completely inactive after 16 h incubation at 50°C. Enzymes immobilized on cyanogen bromide or glyoxyl agarose maintain 100% of their initial activity after 16 h at 50°C. Enzyme immobilized on monoaminoethyl-N-aminoethyl-glutaraldehyde or monoaminoethyl-N-aminoethyl-agarose loses more than 50% of its initial activity after 16 h at 50°C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
using 10% (v/v) glycerol, the enzyme maintains 86% of its initial activity at pH 10.0 after 18 h incubation
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HisTrap column chromatography
-
multiple forms: I, II, II-1 and III-2
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
for expression in Escherichia coli BL21 star DE3 cells
expressed in Escherichia coli BL21(DE3) cells
-
overexpression in Escherichia coli JM105
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
a coupled optical enzyme assay
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hammer-Jespersen, K.; Munch-Petersen, A.
Phosphodeoxyribomutase from Escherichia coli. Purification and some properties
Eur. J. Biochem.
17
397-407
1970
Escherichia coli
Manually annotated by BRENDA team
Munch-Petersen, A.; Nygaard, R.; Hammer-Jespersen, K.; Fiil, N.
Mutants constitutive for nucleoside-catabolizing enzymes in Escherichia coli K12. Isolation characterization and mapping
Eur. J. Biochem.
27
208-215
1972
Escherichia coli
Manually annotated by BRENDA team
Leer, J.C.; Hammer-Jespersen, K.
Multiple forms of phosphodeoxyribomutase from Escherichia coli. Physical and chemical characterization
Biochemistry
14
599-607
1975
Escherichia coli
Manually annotated by BRENDA team
Tozzi, M.G.; Catalani, R.; Ipata, P.L.; Mura, U.
A coupled optical enzyme assay of phosphomutase
Anal. Biochem.
123
265-269
1982
Escherichia coli
Manually annotated by BRENDA team
Barbas, C.F.; Wong, C.H.
Overexpression and substrate specificity studies of phosphodeoxyribomutase and thymidine phosphorylase
Bioorg. Chem.
19
261-269
1991
Escherichia coli
-
Manually annotated by BRENDA team
Hamamoto, T.; Noguchi, T.; Midorikawa, Y.
Phosphopentomutase of Bacillus stearothermophilus TH6-2: the enzyme and its gene ppm
Biosci. Biotechnol. Biochem.
62
1103-1108
1998
Geobacillus stearothermophilus, Escherichia coli, Geobacillus stearothermophilus TH6-2
Manually annotated by BRENDA team
Taverna-Porro, M.; Bouvier, L.A.; Pereira, C.A.; Montserrat, J.M.; Iribarren, A.M.
Chemoenzymic preparation of nucleosides from furanoses
Tetrahedron Lett.
49
2642-2645
2008
Escherichia coli
-
Manually annotated by BRENDA team
Horinouchi, N.; Kawano, T.; Sakai, T.; Matsumoto, S.; Sasaki, M.; Mikami, Y.; Ogawa, J.; Shimizu, S.
Screening and characterization of a phosphopentomutase useful for enzymatic production of 2-deoxyribonucleoside
N. Biotechnol.
26
75-82
2009
Lysinibacillus sphaericus (B3ITC5), Lysinibacillus sphaericus, Escherichia coli (P0A6K6), Escherichia coli, Lysinibacillus sphaericus AKU 229 (B3ITC5)
Manually annotated by BRENDA team
Rivero, C.W.; De Benedetti, E.C.; Gallego, F.L.; Pessela, B.C.; Guisan, J.M.; Trelles, J.A.
Biosynthesis of an antiviral compound using a stabilized phosphopentomutase by multipoint covalent immobilization
J. Biotechnol.
249
34-41
2017
Escherichia coli, Escherichia coli ATCC 4157
Manually annotated by BRENDA team
Meyer, F.; Keller, P.; Hartl, J.; Groeninger, O.G.; Kiefer, P.; Vorholt, J.A.
Methanol-essential growth of Escherichia coli
Nat. Commun.
9
1508
2018
Escherichia coli, Escherichia coli MeSV1
Manually annotated by BRENDA team