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IUBMB CommentsInvolved in the biosynthesis of the C-P bond, although the equilibrium greatly favours phosphoenolpyruvate.
The taxonomic range for the selected organisms is: Mytilus edulis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
pep mutase, phosphoenolpyruvate mutase, phosphoenolpyruvate phosphomutase, pep phosphomutase, peppm, carboxyphosphoenolpyruvate phosphonomutase,
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carboxyphosphoenolpyruvate phosphonomutase
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CPEP phosphonomutase
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PEP phosphomutase
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phosphoenolpyruvate mutase
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phosphoenolpyruvate phosphomutase
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phosphomutase, phosphoenolpyruvate-phosphonopyruvate
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phosphoenolpyruvate = 3-phosphonopyruvate
mechanism
phosphoenolpyruvate = 3-phosphonopyruvate
mechanism
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phosphoenolpyruvate 2,3-phosphonomutase
Involved in the biosynthesis of the C-P bond, although the equilibrium greatly favours phosphoenolpyruvate.
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3-phosphonopyruvate
phosphoenolpyruvate
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r
phosphoenolpyruvate
3-phosphonopyruvate
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r
phosphoenolpyruvate
3-phosphonopyruvate
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r
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additional information
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no activation by Ca2+
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0.0016 - 0.06
3-phosphonopyruvate
0.0016 - 0.054
Phosphonopyruvate
0.0016
3-phosphonopyruvate
wild-type, pH 7.5, 25°C
0.0059
3-phosphonopyruvate
mutant K120R, pH 7.5, 25°C
0.038
3-phosphonopyruvate
mutant N122A, pH 7.5, 25°C
0.046
3-phosphonopyruvate
mutant K120A, pH 7.5, 25°C
0.06
3-phosphonopyruvate
mutant L124A, pH 7.5, 25°C
0.0016
Phosphonopyruvate
25°C, pH 7.5
0.0032
Phosphonopyruvate
mutant N122D, 25°C, pH 7.5
0.0065
Phosphonopyruvate
mutant H190A, 25°C, pH 7.5
0.0078
Phosphonopyruvate
mutant D58N, 25°C, pH 7.5
0.038
Phosphonopyruvate
mutant N122A, 25°C, pH 7.5
0.054
Phosphonopyruvate
mutant R159A, 25°C, pH 7.5
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0.006 - 34
3-phosphonopyruvate
0.006
3-phosphonopyruvate
mutant N122A, pH 7.5, 25°C
0.0098
3-phosphonopyruvate
mutant L124A, pH 7.5, 25°C
0.32
3-phosphonopyruvate
mutant K120R, pH 7.5, 25°C
0.34
3-phosphonopyruvate
mutant K120A, pH 7.5, 25°C
34
3-phosphonopyruvate
wild-type, pH 7.5, 25°C
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0.022
sulfopyruvate
25°C, pH 7.5
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Uniprot
brenda
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PEPM_MYTED
295
0
32912
Swiss-Prot
other Location (Reliability: 1)
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34000
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4 * 34000, SDS-PAGE
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tetramer
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4 * 34000, SDS-PAGE
tetramer
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crystallization data
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of wild-type and mutant D58A, both in apo state and in complex with Mg2+
in complex with Mg2+-oxalate
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K120A
30fold increase in Km-value
K120R
3fold increase in Km-value
L124A
40fold increase in Km-value
D58A
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D58 functions in phosphoryl transfer
D85A
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D85, D87, E114 function in Mg2+-binding
D87A
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D85, D87, E114 function in Mg2+-binding
E114A
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D85, D87, E114 function in Mg2+-binding
R159A
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R159 functions in phosphoenolpyruvate carboxylate binding
D58A
no enzymic activity
D58A
crystallization data
N122A
Km: 0.038 mM
N122A
25fold increase in Km-value
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-80°C, TEA buffer, pH 7.5, 10% glycerol, 4 weeks, minimal losses of activity
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4°C, TEA buffer, pH 7.5, 10% glycerol, 2 weeks, minimal losses of activity
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Huang, K.; Li, Z.; Jia, Y.; Dunaway-Mariano, D.; Herzberg, O.
Helix swapping between two alpha/beta barrels: crystal structure of phosphoenolpyruvate mutase with bound Mg(2+)-oxalate
Structure Fold. Des.
7
539-548
1999
Mytilus edulis
brenda
Liu, S.; Lu, Z.; Jia, Y.; Dunaway-Mariano, D.; Herzberg, O.
Dissociative phosphoryl transfer in PEP mutase catalysis: structure of the enzyme/sulfopyruvate complex and kinetic properties of mutants
Biochemistry
41
10270-10276
2002
Mytilus edulis (P56839), Mytilus edulis
brenda
Kim, A.; Kim, J.; Martin, B.M.; Dunaway-Mariano, D.
Isolation and characterization of the carbon-phosphorus bond-forming enzyme phosphoenolpyruvate mutase from the mollusk Mytilus edulis
J. Biol. Chem.
273
4443-4448
1998
Mytilus edulis
brenda
Jia, Y.; Lu, Z.; Huang, K.; Herzberg, O.; Dunaway-Mariano, D.
Insight into the mechanism of phosphoenolpyruvate mutase catalysis derived from site-directed mutagenesis studies of active site residues
Biochemistry
38
14165-14173
1999
Mytilus edulis
brenda
Liu, S.; Lu, Z.; Han, Y.; Jia, Y.; Howard, A.; Dunaway-Mariano, D.; Herzberg, O.
Conformational flexibility of PEP mutase
Biochemistry
43
4447-4453
2004
Mytilus edulis (P56839)
brenda