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Information on EC 5.4.2.7 - phosphopentomutase and Organism(s) Bacillus cereus and UniProt Accession Q818Z9
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5.4.2.7 phosphopentomutaseIUBMB 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.
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Word Map
- 5.4.2.7
- nucleoside
- purine
- 5-phosphate
- phosphoglucomutase
- deoxyriboaldolase
- 2-deoxyribose
- ribose-5-phosphate
-
nucleobase
- phosphorylases
- deoxyribonucleosides
- 2'-deoxyribonucleoside
- ribokinase
- 1,6-diphosphate
-
phosphorolysis
-
phosphomutases
- analysis
- biotechnology
The taxonomic range for the selected organisms is: Bacillus cereus
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
phosphopentomutase, phosphoribomutase, phosphodeoxyribomutase, deoxyribomutase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-D-Glucose-1,6-bisphosphate:deoxy-D-ribose-1-phosphate phosphotransferase
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-
-
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Deoxyribomutase
-
-
-
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Deoxyribose phosphomutase
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-
-
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Phosphodeoxyribomutase
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-
-
-
Phosphomutase, deoxyribose
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-
-
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Phosphoribomutase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
isomerization
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-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
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-, -
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
9026-77-1
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Ribose 1-phosphate
?
-
inducible enzyme. In order to enter the pentose phosphate cycle ribose 1-phosphate must be isomerized to ribose 5-phosphate
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Ribose 1-phosphate
?
-
inducible enzyme. In order to enter the pentose phosphate cycle ribose 1-phosphate must be isomerized to ribose 5-phosphate
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mn2+
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-Glucose 1,6-bisphosphate
there is a concentration-dependent enhancement of PPM activity between 0.0001 mM and 0.0025 mM D-glucose 1,6-bisphosphate
glucose 1,6-bisphosphate
required for activation. The conformational change in Lys240 alters the affinity of the enzyme for the activator
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.263
D-ribose 5-phosphate
in 25 mM Tris-HCl, pH 8.0, and 0.1 mM MnCl2, 0.0005 mM glucose 1,6-bisphosphate,at 23°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
10.2
D-ribose 5-phosphate
in 25 mM Tris-HCl, pH 8.0, and 0.1 mM MnCl2, 0.0005 mM glucose 1,6-bisphosphate,at 23°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the active site is located between two independently folded domains. The enzyme engages substrates when the active site nucleophile, Thr85, is phosphorylated
additional information
-
the active site is located between two independently folded domains. The enzyme engages substrates when the active site nucleophile, Thr85, is phosphorylated
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the active site is located between two independently folded domains
additional information
-
the active site is located between two independently folded domains
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphoprotein
phosphorylation of the active site nucleophile, Thr85, activates the enzyme, structure comparison of activated phosphorylated and unactivated unphosphorylated enzymes, phosphorylation-dependent interdomain orientation, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme alone, co-crystallized with ribose 5-phosphate, co-crystallized with glucose 1,6-bisphosphate, and following activation with glucose 1,6-bisphosphate, hanging drop vapor diffusion method, using 100 mM Bis-Tris, pH 5.5, 50 mM MnCl2, 14% (w/v) polyethylene glycol 3350, and 75 mM NH4CH3COO
purified recombinant detagged wild-type and mutant T85Q and T85E enzymes free or in complex with glucose 1,6-bisphosphate, hanging drop vapor diffusion method, for the free enzyme crystals: mixing of 10 mg/ml protein in 25mM Tris-HCl, pH 7.5, and 1 mM MnCl2, with reservoir solution containing 100 mM Bis-Tris, pH 5.5, 50 mM MnCl2, 17% PEG 3350 (wild-type) or 13% PEG 3350 (mutant T85Q), and 75 mM NH4CH3COO, for the complex crystals: mixing of 10 mg/ml protein in 5 mM glucose 1,6-bisphosphate, 25 mM Tris-HCl, pH 7.4, and 1 mM MnCl2 with a reservoir solution containing 100 mM Bis-Tris, pH 5.5, 50 mM MnCl2, 14% PEG 3350, and 50 mM NH4CH3COO, X-ray diffraction structure determination and analysis at 1.8-2.3 A resolution
hanging drop vapor diffusion method, using 100 mM Bis-Tris pH 5.5, 50 mM MnCl2, 13-16% PEG 3350, and 25-100 mM NH4CH3COO
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hanging drop vapor diffusion method, using 100 mM Bis-Tris pH 5.5, 50 mM MnCl2, 13-16% PEG 3350, and 25-100 mM NH4CH3COO
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D156A
site-directed mutagenesis, the D156A variant displays a dramatically reduced level of phosphorylation of the active site Thr85 compared to the wild-type, and does not acquire phosphatase activity
K240A
site-directed mutagenesis, the K240A variant can be phosphorylated by the small molecule activator glucose 1,6-bisphosphate like the wild-type enzyme
T85E
site-directed mutagenesis, the T85E variant mimics the active site charge of the activated state of the enzyme, the affinity for activator glucose 1,6-bisphosphate is 4.5fold reduced compared to the wild-type enzyme
T85Q
site-directed mutagenesis, the T85Q variant mimics the active site charge of the unactivated state of the enzyme, the affinity for activator glucose 1,6-bisphosphate is only slightly reduced compared to the wild-type enzyme
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the phosphoenzyme is stable throughout purification and crystallization
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, His-tag removal by thrombin cleavage, followed by gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ipata, P.L.; Sgarrella, F.; Catalani, R.; Tozzi, M.G.
Induction of phosphoribomutase in Bacillus cereus growing on nucleosides
Biochim. Biophys. Acta
755
253-256
1983
Bacillus cereus
Panosian, T.D.; Nannemann, D.P.; Bachmann, B.O.; Iverson, T.M.
Crystallization and preliminary X-ray analysis of a phosphopentomutase from Bacillus cereus
Acta Crystallogr. Sect. F
66
811-814
2010
Bacillus cereus, Bacillus cereus ATCC 14579D
Panosian, T.D.; Nannemann, D.P.; Watkins, G.R.; Phelan, V.V.; McDonald, W.H.; Wadzinski, B.E.; Bachmann, B.O.; Iverson, T.M.
Bacillus cereus phosphopentomutase is an alkaline phosphatase family member that exhibits an altered entry point into the catalytic cycle
J. Biol. Chem.
286
8043-8054
2011
Bacillus cereus (Q818Z9), Bacillus cereus, Bacillus cereus ATCC 14579 (Q818Z9)
Iverson, T.M.; Panosian, T.D.; Birmingham, W.R.; Nannemann, D.P.; Bachmann, B.O.
Molecular differences between a mutase and a phosphatase: investigations of the activation step in Bacillus cereus phosphopentomutase
Biochemistry
51
1964-1975
2012
Bacillus cereus (Q818Z9), Bacillus cereus, Bacillus cereus DSM 31 (Q818Z9)
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