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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 7.6.2.1 - P-type phospholipid transporter and Organism(s) Escherichia coli and UniProt Accession P60752

for references in articles please use BRENDA:EC7.6.2.1
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. Different forms of the enzyme move phospholipids such as phosphatidylcholine, lyso-phosphatidylcholine, phosphatidylserine, phosphatidylethanolamine, phosphatidyglycerol, sphingomyelin and glucosylceramide from one membrane face to the other ('flippase').
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Escherichia coli
UNIPROT: P60752
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: Escherichia coli
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
Synonyms
mg2+-atpase, abcb4, flippase, plscr1, atp8b1, scramblase, aminophospholipid translocase, ala12, tat-2, drs2p, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
lipid flippase
-
aminophospholipid flippase
-
-
-
-
aminophospholipid flippase 10
-
-
-
-
aminophospholipid flippase 11
-
-
-
-
aminophospholipid flippase 12
-
-
-
-
aminophospholipid translocase
-
-
-
-
aminophospholipid translocase VC
-
-
-
-
ATPase II
-
-
-
-
ATPVC
-
-
-
-
ATPVD
-
-
-
-
flippase
-
-
-
-
HUSSY-20
-
-
-
-
Mg2+-ATPase
-
-
-
-
Mg2+-ATPase A
-
-
-
-
peptidoglycan lipid II flippase
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
transmembrane transport
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (P-type, phospholipid-flipping)
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. Different forms of the enzyme move phospholipids such as phosphatidylcholine, lyso-phosphatidylcholine, phosphatidylserine, phosphatidylethanolamine, phosphatidyglycerol, sphingomyelin and glucosylceramide from one membrane face to the other ('flippase').
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + H2O + Lipid A/in
ADP + phosphate + Lipid A/out
show the reaction diagram
-
-
-
?
ATP + H2O + phosphatidylethanolamine/in
ADP + phosphate + phosphatidylethanolamine/out
show the reaction diagram
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
peptidoglycan lipid II/out
peptidoglycan lipid II/in
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
MurJ is required for peptidoglycan biogenesis in Eschrichia coli
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
MurJ is required for peptidoglycan biogenesis in Eschrichia coli
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
AlFx
trapping of MsbA with 0.8 mM AlFx results in incomplete inhibition of activity
BeFx
trapping of MsbA with 0.8 mM BeFx results in incomplete inhibition of activity
lipid A
lipid A inhibits translocation by approx. 30% at 0.01-0.04 mg/ml
phosphate analogue Vi
the presence of 0.1-0.2 m M Vi inhibits flippase activity of MsbA by approx. 50%
vanadate
-
maximal half-inhibition at 0.035 mM
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
flippase activity is essentially supported only by ATP. If the ATP concentration in the assay falls below 5 mM, there is a significant decrease in flippase activity. Maximal translocation occurs at 10 mM ATP
Kdo2-lipid A
-
-
Phospholipids
-
The activity of purified MsbA is dependent upon the presence of phospholipids.
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.878
ATP
-
pH 7.5, 37°C, KM value of purified, detergent-solubilized MsbA, whereas the KM value calculated in the presence of 0.05 mM KdO2-lipid A is decreased by more than half
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.002 - 0.004
-
activity of purified, detergent-solubilized MsbA
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8.5
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65000
2 * 65000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
2 * 65000, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A270T
-
mutant and wild-type enzymes have similar activities at 30°C, but the mutant activity is decreased significant at 42°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography
recombinant wild-type and mutant enzymes
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
the gene MsbA is cloned into pET28b behind the T7 promoter in-frame with an N-terminal His6tag
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Doerrler, W.T.; Raetz, C.R.
ATPase activity of the MsbA lipid flippase of Escherichia coli
J. Biol. Chem.
277
36697-36705
2002
Escherichia coli
Manually annotated by BRENDA team
Ruiz, N.
Bioinformatics identification of MurJ (MviN) as the peptidoglycan lipid II flippase in Escherichia coli
Proc. Natl. Acad. Sci. USA
105
15553-15557
2008
Escherichia coli
Manually annotated by BRENDA team
Eckford, P.D.; Sharom, F.J.
The reconstituted Escherichia coli MsbA protein displays lipid flippase activity
Biochem. J.
429
195-203
2010
Escherichia coli (P60752), Escherichia coli
Manually annotated by BRENDA team