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4.2.1.11: phosphopyruvate hydratase

This is an abbreviated version!
For detailed information about phosphopyruvate hydratase, go to the full flat file.

Word Map on EC 4.2.1.11

Reaction

2-phospho-D-glycerate
=
phosphoenolpyruvate
 +
H2O

Synonyms

14-3-2 protein, 2-phospho-D-glycerate hydro-lyase, 2-phospho-D-glycerate hydrolase, 2-phospho-D-glycerate hydrolyase, 2-phospho-D-glyceratehydrolyase, 2-phosphoglycerate dehydratase, 2-phosphoglycerate enolase, 2-phosphoglycerate hydrolase, 2-phosphoglycerate hydrolyase, 2-phosphoglyceric dehydratase, 2-phosphopyruvate hydrolyase, alpha,alpha-enolase, alpha-enolase, alpha-enolase 1, alpha-enolase 2, Alt a XI, beta,beta-enolase, beta-enolase, Cla h VI, Csenolase, cytotoxin B, EhENO, ENO, ENO-1, Eno-alpha, ENO-S, ENO1, Eno1p, Eno2, ENOA, EnoA I, EnoA1, ENOL, Enol-1, enolase, enolase 1, enolase 2, enolase alpha, enolase gamma, enolase S, enolase-1, enolase-alpha, enolase-beta, Enolase-phosphatase E1, enolase2p, Err2p, Err3p, gamma,gamma-enolase, gamma-enolase, hENO1, HLE1, human alpha-enolase, human neuron-specific enolase, hydratase, phosphoenolpyruvate, Laminin binding protein, Major allergen Alt a 11, MASA, MSE, Neural enolase, neuron specific enolase, neuron-specific enolase, neuronal enolase, NNE, Non-neural enolase, NSE, OSE1, p45, P46, Pfen, Pfeno, phosphoenolpyruvate enolase, phosphoenolpyruvate hydratase, Phosphopyruvate hydratase, plasminogen-binding alpha-enolase, R-NSE, r-Pfen, rBaEn, rSsEno, SEN, SjENO, Skeletal muscle enolase, SPM2, SsEno, SSO0913, streptococcal surface enolase, Tau-crystallin, tv-ENO1, tv-rENO1, XEP, yeast enolase

ECTree

     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.11 phosphopyruvate hydratase

Engineering

Engineering on EC 4.2.1.11 - phosphopyruvate hydratase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K147A
requires a 10fold greater concentration of protein for observation of enolization
K173A
detectable activity of about 3% of that of wild-type enolase, retains ability to enolize the desthio substrate
K98A
unable to catalyze the enolase reaction
D257K
-
the mutation has no effect on excystation
H389Q/R390S
-
the mutations significantly inhibit excystation
K255A
-
while the binding activity of the mutated protein is drastically reduced, the residual enzymatic activity is more than 50% of the wild type enzyme
K259A K255A
-
while the binding activity of the mutated protein is drastically reduced, the residual enzymatic activity is more than 50% of the wild type enzyme
K259A/K422A K255A
-
while the binding activity of the mutated protein is drastically reduced, the residual enzymatic activity is more than 50% of the wild type enzyme
K422A K255A
-
while the binding activity of the mutated protein is drastically reduced, the residual enzymatic activity is more than 50% of the wild type enzyme
K255A
-
while the binding activity of the mutated protein is drastically reduced, the residual enzymatic activity is more than 50% of the wild type enzyme
-
K259A K255A
-
while the binding activity of the mutated protein is drastically reduced, the residual enzymatic activity is more than 50% of the wild type enzyme
-
K259A/K422A K255A
-
while the binding activity of the mutated protein is drastically reduced, the residual enzymatic activity is more than 50% of the wild type enzyme
-
K422A K255A
-
while the binding activity of the mutated protein is drastically reduced, the residual enzymatic activity is more than 50% of the wild type enzyme
-
E414L
E168Q
E211Q
G157D
correctly folded, less stable than wild-type enolase, dissociation into subunit forms accelerated
G376E
correctly folded, less stable than wild-type enolase, dissociation into subunit forms accelerated
H159A
H159F
-
less than 1% of the activity compared to the wild type
H159G
-
inactive form
H159N
-
less than 1% of the activity compared to the wild type
K345A
K345A/N80D/N126D
heterodimer with one inactive K345A subunit and one active N80D and N126D subunit
N207A
-
50% of the activity compared to the wild type
N80D/N126D
mutant with surface mutations to facilitate ion-exchange chromatographic separation
deltaK433/K434
mutant with different oligomerization state
K433L/K434L
mutant with different oligomerization state
K434L
mutant with different oligomerization state
DELTA434-435
-
mutant with decreased Glu- and Lys-plasminogen-binding activities
F137L/E363G
-
the dimer-dimer interface mutant destabilizes the octameric structure, the double mutant is more easily dissociated in the presence of NaClO4 than is the wild type
K434L/K435L
-
mutant with decreased Glu- and Lys-plasminogen-binding activities
K435L
-
mutant with decreased Glu- and Lys-plasminogen-binding activities
additional information