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Information on EC 5.4.2.6 - beta-Phosphoglucomutase and Organism(s) Lactococcus lactis and UniProt Accession P71447
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5.4.2.6 beta-PhosphoglucomutaseIUBMB Comments
The enzyme requires Mg2+ and phosphorylation of an aspartate residue at the active site. The enzyme is able to autophosphorylate itself with its substrate beta-D-glucose 1-phosphate. Although this is a slow reaction, only a single turnover is required for activation. Once the phosphorylated enzyme is formed, it generates the reaction intermediate beta-D-glucose 1,6-bisphosphate, which can be used to phosphorylate the enzyme in subsequent cycles . cf. EC 5.4.2.2, phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent).
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Word Map
- 5.4.2.6
- 1-phosphate
- lactis
- maltose
-
phosphorane
-
dehalogenase
- trehalose
- 1,6-bisphosphate
-
haloacid
-
lactococci
- alpha-glucose
- analysis
The taxonomic range for the selected organisms is: Lactococcus lactis
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
beta-phosphoglucomutase, beta-pgm, betapgm, tm1254, pspgm, py04_1503, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
beta-PGM
Phosphomutase, beta-glucose
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beta-PGM
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
beta-D-Glucose 1-phosphate = beta-D-glucose 6-phosphate
a single Mg2+ coordination site accomodates water, phosphate, and the phosphorane intermediate during catalytic turnover. Bi-bi ping-pong mechanism, substrate induced-fit mechanism allows phosphomutase activity to dominate over the intrinsic phosphatase activity
beta-D-Glucose 1-phosphate = beta-D-glucose 6-phosphate
mechanism is a nucleophilic substitution via an associative pathway, enzyme stablizes the phosphorane intermediate along that pathway
beta-D-Glucose 1-phosphate = beta-D-glucose 6-phosphate
phosphoryl transfer rather than ligand binding is rate-limiting. Beta-D-glucose 1,6-bisphosphate is a reaction intermediate and binds to the active site in two different orientations with roughly the same efficiency. Reorientation of the beta-D-glucose 1,6-bisphosphate intermediate occurs by diffusion into solvent followed by binding in the opposite orientation
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beta-D-Glucose 1-phosphate = beta-D-glucose 6-phosphate
reaction mechanism of the phosphoryl transfer starting from the bisphosphate intermediate beta-D-glucose-1,6-(bis)phosphate in both directions of the reversible reaction, overview. The calculated energy barrier of the reaction for the beta-D-glucose 1-phosphate to beta-D-glucose 1,6-diphosphate step is only slightly higher than for the beta-G1,6diP to beta-G6P step. Residues Ser114 and Lys145 and Mg2+ play important roles in stabilizing the large negative charge on the phosphate through strong coordination with the phosphate oxygens and guiding the phosphate group throughout the catalytic process
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
isomerization
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SYSTEMATIC NAME
IUBMB Comments
beta-D-Glucose 1,6-phosphomutase
The enzyme requires Mg2+ and phosphorylation of an aspartate residue at the active site. The enzyme is able to autophosphorylate itself with its substrate beta-D-glucose 1-phosphate. Although this is a slow reaction, only a single turnover is required for activation. Once the phosphorylated enzyme is formed, it generates the reaction intermediate beta-D-glucose 1,6-bisphosphate, which can be used to phosphorylate the enzyme in subsequent cycles [4]. cf. EC 5.4.2.2, phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent).
CAS REGISTRY NUMBER
COMMENTARY
68651-99-0
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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
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
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r
beta-D-Glucose 1-phosphate
beta-D-Glucose 6-phosphate
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via stabile intermediate beta-D-glucose-1,6-(bis)phosphate
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r
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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Co2+
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activation at 1 mM, efficiency of activation in descending order, Co2+, Mn2+, Mg2+ and Ni2+
Mg2+
Mn2+
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activation at 1 mM, efficiency of activation in descending order, Co2+, Mn2+, Mg2+ and Ni2+
Ni2+
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activation at 1 mM, efficiency of activation in descending order, Co2+, Mn2+, Mg2+ and Ni2+
Mg2+
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activation at 1 mM, efficiency of activation in descending order, Co2+, Mn2+, Mg2+ and Ni2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
F-
formation of a MgF3- transition state analogue when glucose 6-phosphate, magnesium, and fluoride are present with the enzyme, in which MgF3- mimics the transferring PO3- moiety
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
beta-D-glucose 1,6-bisphosphate
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required, Km value 0.0065 mM. Beta-D-glucose 1,6-bisphosphate is a reaction intermediate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0045
beta-D-glucose 1-phosphate
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in the presence of beta-D-glucose 1,6-diphosphate and Mg2+
0.0147
beta-D-glucose 1-phosphate
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in 50 mM buffer (HEPES, pH 7.2), with 2 mM MgCl2
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
17
beta-D-glucose 1-phosphate
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in the presence of beta-D-glucose 1,6-diphosphate and Mg2+
64.7
beta-D-glucose 1-phosphate
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in 50 mM buffer (HEPES, pH 7.2), with 2 mM MgCl2
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
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
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fluoromagnesate and fluoroaluminate complexes of beta-phosphoglucomutase demonstrate the importance of charge balance in transition-state stabilization for phosphoryl transfer enzymes, overview
additional information
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reaction mechanism analysis by docking techniques and QM/MM theoretical method, overview. Residues Ser114 and Lys145 and Mg2+ play important roles in stabilizing the large negative charge on the phosphate through strong coordination with the phosphate oxygens and guiding the phosphate group throughout the catalytic process
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
catalysis of reaction proceeds via a phosphoenzyme form
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
both in complex with inhibitor alpha-D-galactose 1-phosphate or substrate beta-D-glucose 1-phosphate
characterization of the solution structure of the MgF3- complex bound to the enzyme active site
crystals of phosphorylated native beta-PGM are grown at pH 7.5 in the presence of 5 M Mg2+ using the vapor-diffusion method with hanging drop geometry, 100 mM ammonium fluoride and 16% polyethylene glycol 3350 are used as precipitating agents, crystals diffrakt to 2.3 A
beta-PGM is transferred to 1 mM HEPES, pH 7.5, 10 mM MgCl2 and 0.1 mM dithiothreitol, final beta-PGM concentration at 15 mg/ml, crystals are obtained from either 150 mM ammonium acetate, 100 mM trisodium citrate dihydrate, pH 4.5, 25% polyethylene glycol 4000 or 100 mM ammonium fluoride, 16% polyethylene glycol 3350 by hanging-drop vapor diffusion, crystals of selenium methionyl-substituted beta-PGM diffract to 2.3 A
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purified recombinant enzyme in complex with transition-state analogue fluoromagnesate and glucose 6-phosphate or ground-state analogue fluoroaluminate and glucose 6-phosphate, sitting drop vapour diffusion method, mixing of 15 mg/mL 50 mM K+ HEPES, pH 7.2, 5 mM MgCl2, 1 mM azide, 0.1 mM DTT, 10 mM NH4F, and 10 mM BeCl2 1:1 with the precipitant containing 26-30% w/v PEG 4000, 200 mM Na acetate, and 100 mM Tris, pH 7.5, X-ray diffraction structure determination and analysis at 1.65 A resolution, molecular replacement
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression of native and selenomethionyl beta-PGM in escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nakamura, K.; Shirokane, Y.; Suzuki, M.
Purification and some properties of beta-phosphoglucomutase from Lactobacillus lactis subsp. cremonis IFP 3427
J. Ferment. Bioeng.
85
350-353
1998
Lactobacillus delbrueckii subsp. lactis, Lactococcus lactis
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Lahiri, S.D.; Zhang, G.; Radstrom, P.; Dunaway-Mariano, D.; Allen, K.N.
Crystallization and preliminary X-ray diffraction studies of beta-phosphoglucomutase from Lactococcus lactus
Acta Crystallogr. Sect. D
58
324-326
2002
Lactococcus lactis
Lahiri, S.D.; Zhang, G.; Dunaway-Mariano, D.; Allen, K.N.
Caught in the act: the structure of phosphorylated beta-phosphoglucomutase from Lactococcus lactis
Biochemistry
41
8351-8359
2002
Lactococcus lactis (P71447), Lactococcus lactis
Zhang, G.; Dai, J.; Wang, L.; Dunaway-Mariano, D.; Tremblay, L.W.; Allen, K.N.
Catalytic cycling in beta-phosphoglucomutase: a kinetic and structural analysis
Biochemistry
44
9404-9416
2005
Lactococcus lactis (P71447), Lactococcus lactis
Tremblay, L.W.; Zhang, G.; Dai, J.; Dunaway-Mariano, D.; Allen, K.N.
Chemical confirmation of a pentavalent phosphorane in complex with beta-phosphoglucomutase
J. Am. Chem. Soc.
127
5298-5299
2005
Lactococcus lactis (P71447)
Dai, J.; Wang, L.; Allen, K.N.; Radstrom, P.; Dunaway-Mariano, D.
Conformational cycling in beta-phosphoglucomutase catalysis: reorientation of the beta-D-glucose 1,6-(bis)phosphate intermediate
Biochemistry
45
7818-7824
2006
Lactococcus lactis
Baxter, N.J.; Olguin, L.F.; Golicnik, M.; Feng, G.; Hounslow, A.M.; Bermel, W.; Blackburn, G.M.; Hollfelder, F.; Waltho, J.P.; Williams, N.H.
A Trojan horse transition state analogue generated by MgF3- formation in an enzyme active site
Proc. Natl. Acad. Sci. USA
103
14732-14737
2006
Lactococcus lactis (P71447)
Baxter, N.J.; Blackburn, G.M.; Marston, J.P.; Hounslow, A.M.; Cliff, M.J.; Bermel, W.; Williams, N.H.; Hollfelder, F.; Wemmer, D.E.; Waltho, J.P.
Anionic charge is prioritized over geometry in aluminum and magnesium fluoride transition state analogs of phosphoryl transfer enzymes
J. Am. Chem. Soc.
130
3952-3958
2008
Lactococcus lactis
Golicnik, M.; Olguin, L.F.; Feng, G.; Baxter, N.J.; Waltho, J.P.; Williams, N.H.; Hollfelder, F.
Kinetic analysis of beta-phosphoglucomutase and its inhibition by magnesium fluoride
J. Am. Chem. Soc.
131
1575-1588
2009
Lactococcus lactis
Elsaesser, B.; Dohmeier-Fischer, S.; Fels, G.
Theoretical investigation of the enzymatic phosphoryl transfer of beta-phosphoglucomutase: revisiting both steps of the catalytic cycle
J. Mol. Model.
18
3169-3179
2012
Lactococcus lactis
Griffin, J.L.; Bowler, M.W.; Baxter, N.J.; Leigh, K.N.; Dannatt, H.R.; Hounslow, A.M.; Blackburn, G.M.; Webster, C.E.; Cliff, M.J.; Waltho, J.P.
Near attack conformers dominate beta-phosphoglucomutase complexes where geometry and charge distribution reflect those of substrate
Proc. Natl. Acad. Sci. USA
109
6910-6915
2012
Lactococcus lactis
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