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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 5.4.2.9 - phosphoenolpyruvate mutase and Organism(s) Mytilus edulis and UniProt Accession P56839

for references in articles please use BRENDA:EC5.4.2.9
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)
                5.4.2.9 phosphoenolpyruvate mutase
IUBMB Comments
Involved in the biosynthesis of the C-P bond, although the equilibrium greatly favours phosphoenolpyruvate.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Mytilus edulis
UNIPROT: P56839
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
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, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxyphosphoenolpyruvate phosphonomutase
-
-
-
-
CPEP phosphonomutase
-
-
-
-
PEP mutase
-
-
-
-
PEP phosphomutase
-
-
-
-
PEPPM
-
-
-
-
phosphoenolpyruvate mutase
-
-
-
-
phosphoenolpyruvate phosphomutase
-
-
-
-
phosphomutase, phosphoenolpyruvate-phosphonopyruvate
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
phosphoenolpyruvate = 3-phosphonopyruvate
show the reaction diagram
mechanism
phosphoenolpyruvate = 3-phosphonopyruvate
show the reaction diagram
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isomerization
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
phosphoenolpyruvate 2,3-phosphonomutase
Involved in the biosynthesis of the C-P bond, although the equilibrium greatly favours phosphoenolpyruvate.
CAS REGISTRY NUMBER
COMMENTARY hide
115756-49-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-phosphonopyruvate
phosphoenolpyruvate
show the reaction diagram
-
-
-
r
phosphoenolpyruvate
3-phosphonopyruvate
show the reaction diagram
-
-
-
r
phosphoenolpyruvate
3-phosphonopyruvate
show the reaction diagram
-
-
-
r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
Km: 0.0003 mM
Mg2+
-
Km: 0.004 mM
Mn2+
-
Km: 0.00011 mM
Ni2+
-
Km: 0.0022 mM
Zn2+
-
Km: 0.00018
additional information
-
no activation by Ca2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
sulfopyruvate
-
Mg2+-oxalate
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0016 - 0.06
3-phosphonopyruvate
0.0016 - 0.054
Phosphonopyruvate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.006 - 34
3-phosphonopyruvate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.022
sulfopyruvate
25°C, pH 7.5
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PEPM_MYTED
295
0
32912
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
144000
-
gel filtration
34000
-
4 * 34000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
of wild-type and mutant D58A, both in apo state and in complex with Mg2+
in complex with Mg2+-oxalate
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D58N
Km: 0.0078 mM
D58S
no enzymic activity
H190A
Km: 0.0065 mM
K120A
30fold increase in Km-value
K120R
3fold increase in Km-value
L124A
40fold increase in Km-value
N122A
N122D
Km: 0.0032 mM
R159A
Km: 0.054 mM
D58A
-
D58 functions in phosphoryl transfer
D85A
-
D85, D87, E114 function in Mg2+-binding
D87A
-
D85, D87, E114 function in Mg2+-binding
E114A
-
D85, D87, E114 function in Mg2+-binding
R159A
-
R159 functions in phosphoenolpyruvate carboxylate binding
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, TEA buffer, pH 7.5, 10% glycerol, 4 weeks, minimal losses of activity
-
4°C, TEA buffer, pH 7.5, 10% glycerol, 2 weeks, minimal losses of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team