Information on EC 3.6.3.2 - Mg2+-importing ATPase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY hide
3.6.3.2
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RECOMMENDED NAME
GeneOntology No.
Mg2+-importing ATPase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + Mg2+/out = ADP + phosphate + Mg2+/in
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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-
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transmembrane transport
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (Mg2+-importing)
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme occurs in both Gram-positive and Gram-negative bacteria, and three types are known, designated as CorA, MgtA and MgtB. The CorA itself is not an ATPase but an Mg2+ transporter.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene mgtE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
periplasmic domain, expression in Escherichia coli
Swissprot
Manually annotated by BRENDA team
strain OF4, gene mgtE
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Manually annotated by BRENDA team
strain OF4, gene mgtE
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
gene mgtC
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Manually annotated by BRENDA team
gene mgtC
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Manually annotated by BRENDA team
Charles River male mice
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-
Manually annotated by BRENDA team
gene mgtC
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
gene mgtE
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Manually annotated by BRENDA team
strain S4, a multimetal resistant bacterium, gene corA
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Manually annotated by BRENDA team
strain S4, a multimetal resistant bacterium, gene corA
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Manually annotated by BRENDA team
serovar typhimurium
UniProt
Manually annotated by BRENDA team
serovar typhimurium
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-
Manually annotated by BRENDA team
gene mgtE
SwissProt
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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 + Co2+/in
ADP + phosphate + Co2+/out
show the reaction diagram
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apparent dissociation constant: wild-type, 0.0298 mM, recombinant periplasmic domain, 0.0236 mM
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-
?
ATP + H2O + Co2+/out
ADP + phosphate + Co2+/in
show the reaction diagram
ATP + H2O + Mg2+/in
ADP + phosphate + Mg2+/out
show the reaction diagram
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apparent dissociation constant: wild-type, 0.0184 mM, recombinant periplasmic domain, 0.0309 mM9
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-
?
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
show the reaction diagram
ATP + H2O + Ni2+/in
ADP + phosphate + Ni2+/out
show the reaction diagram
ATP + H2O + Ni2+/out
ADP + phosphate + Ni2+/in
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + H2O + Mg2+/out
ADP + phosphate + Mg2+/in
show the reaction diagram
ATP + H2O + Ni2+/out
ADP + phosphate + Ni2+/in
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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activates
additional information
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no or poor inhibition of CorA by Ca2+, Sr2+, Ba2+, Zn2+, Fe2+, and Fe3+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cetyltrimethylammonium bromide
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Mg2+-ATPase activity of ECF1 is very resistant to inhibition by cationic detergents melittin and cetyltrimethylammonium bromide, lower concentrations of cetyltrimethylammonium bromide stimulate Mg2+-ATPase activity of ECF1. MgATP protects, overview
Co(III) hexaamines
inhibit Mrs2p and CorA, inhibition of Ni2+ uptake by CorA
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cobalt(III) hexaamine
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cobalt(III)-hexaamine
cobalt(III)-hexaammine
inhibits Mrs2p channels
cobalt(III)chloropentaamine
cysteine
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inhibits the Mg2+-ATPase activity by 15%, in addition with lanthanum by 25%
dimethyl sulfoxide
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lanthanum
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inhibits the Mg2+-ATPase activity by 8%, not reversible but increased by Cys co-administration to 25% inhibition
oligomycin
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partly inhibited by oligomycin
ruthenium (III) hexaamines
inhibit Mrs2p and CorA, inhibition of Ni2+ uptake by CorA
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ruthenium(II)-hexaamine
ruthenium(III)-hexaamine
ruthenium(III)chloropentaamine
Sr2+
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inhibition of MgtE
strictosamide
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the main glycoalkaloid of Sarcocephalus latifolius leaves and roots, isolated from an ethanolic extract, used as medicinal plant in folk medicine, inhibits the enzyme in vitro and in vivo in kidney, but not in brain, by 45% at 2 mg/ml
thapsigargin
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tributyltin
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TBT, one of the most toxic lipophilic aquatic pollutants. Maximal inhibition of 82% in the gills and 74% in the mantle at 0.00062 mM TBT, non-cooperative inhibition kinetics and a non-competitive mechanism with respect to ATP substrate, via formation of a TBT-Mg-ATPase complex, apparently more stable in the gills than in the mantle
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cetyltrimethylammonium bromide
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i.e. CTAB, Mg2+-ATPase activity of ECF1 is very resistant to inhibition by cetyltrimethylammonium bromide, lower concentrations of cetyltrimethylammonium bromide stimulate Mg2+-ATPase activity of ECF1
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.5 - 2.8
ATP
0.02 - 0.08
Co2+
0.006 - 0.05
Mg2+
0.002 - 0.4
Ni2+
additional information
additional information
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05 - 30
Ca2+
0.008 - 0.04
Co2+
0.03 - 0.07
Mn2+
0.2
Ni2+
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pH 7.4, 37C, MgtE, above
0.08
Sr2+
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pH 7.4, 37C, MgtE
0.12 - 0.17
tributyltin
0.007 - 0.02
Zn2+
additional information
additional information
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inhibition kinetics, the inhibition by tributyltin follows a noncooperative kinetics in both tissues, gill and mantle
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01 - 0.025
Cetyltrimethylammonium bromide
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0000001
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enzyme activity in kidney tissue
0.00000013
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enzyme activity in brain tissue
0.09
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brain Mg2+-ATPase in presence of Cys and lanthanum
0.119
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brain Mg2+-ATPase activity
0.121
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brain Mg2+-ATPase
0.25
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gill enzyme
0.5
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mantle enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
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assay at
8
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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mature, MGT9
Manually annotated by BRENDA team
Madin-Darby kidney cell, basolateral localization of both endogenous and ectopically expressed transporter CNNM4. Single knockdown of my1B, a cargo-recognition subunit of AP-1B, does not affect basolateral localization, but simultaneous knockdown of the my1A subunit of AP-1A abrogates localization
Manually annotated by BRENDA team
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vascular tissue
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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Mrs2 is the major transport protein for Mg2+ uptake into mitochondria
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55000
x * 55000, about, recombinant HA-tagged wild-type and mutant enzymes, SDS-PAGE
102000
105000
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two-dimensional SDS-PAGE
132000
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gel filtration, recombinant periplasmic domain
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
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SDS-PAGE
oligomer
Alr1p is at least a tetramer, Alr1p and Alr2p form homooligomers, but heteroligomers when overexpressed, the oligomerization of Alr1p results in a dominant negative action on the protein; Alr2p forms homooligomers, but heteroligomers when overexpressed
pentamer
tetramer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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disulfide bonds do not participate in tetramer formation
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
periplasmic domain of recombinant enzyme
single particle electron microscopy of recombinant periplasmic domain, enzyme is a pyramid-like homotetramer with a central cavity
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both full-length enzyme and isolated cytoplasmic domain. Enzyme forms a funnel-shaped homopentamer with two transmembrane domains per monomer. An Mg2+ ion is bound between monomers at a conserved site in the cytoplasmic domain
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crystal structure analysis from PDB ID BBJ2 at 3.9 A resolution for the whole enzyme, and at 1.8 A resolution for the soluble domain, overview
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crystal structure analysis, X-ray structure determination at 3.9 A resolution, PDB ID 2BBJ, overview
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enzyme forms a pentameric cone-shaped structure with regulatory metal binding sites in the N-terminal domain
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free wild-type CorA, CorA1-351, and SeMet-AfCorA1-263, in complex with several different metal ions, 15 mg/ml purified CorA1-351 in 20 mM Tris pH 8.0, 100 mM NaCl, 1 mM TCEP, with or without 0.026% n-dodecyl-beta-D-maltoside, with precipitant vapor-diffusion over 20% PEG 400, 0.2 M CaCl2, 0.1 M HEPES, pH 7.0, 40 mg/ml native and SeMet-AfCorA1-263 from 1.3 M ammonium sulfate, 10 mM CoCl2, 0.1 M HEPES, pH 7.4, X-ray diffraction structure determination and analysis at 3.7 A resolution
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recombinant enzyme, purification omits the isolation and subsequent solubilization of the membrane fraction
selenomethionine-labeled full-length enzyme and soluble cytosolic domain in presence and absence of Mg2+, 10 mg/ml full-length protein with 0.1% dodecylmaltoside, by vapour diffusion over 32-34% 2-methyl-2,4-pentanediol, 40 mM magnesium acetate, and 100 mM MES, pH 6.0, cytosolic domain with bound Mg2+ by vapour diffusion over solutions containing 18-22% PEG 400, 0.2M MgCl2, and 0.1M HEPES, pH 7.4, or cytosolic domain in the absence of Mg2+ in 20% PEG 3350, 0.2 M ammonium acetate, and 0.5% octyl-beta-D-glucopyranoside, X-ray diffraction structure determination at 2.3-3.9 A resolution, multiple anomaleous dispersion method
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
Mutants defective in phoP or in both mgtA and mgtB are hypersensitive to oxidative stress-dependent Fe(II)-mediated killing
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656828
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme partially by mitochondria preparation
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native enzyme partially from hearts by mitochondria preparation
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periplasmic domain of recombinant enzyme
recombinant enzyme, purification omits the isolation and subsequent solubilization of the membrane fraction
recombinant HA-tagged wild-type and mutant enzymes in yeast, native enzyme partially by preparation of mitochondria
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 by nickel affinity chromatography, cleavage of the His-tag, and gel filtration to homogeneity
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recombinant N-terminally His-tagged cytosolic domain by nickel affinity chromatography, tag cleavage by thrombin, anion exchange chromatography and gel filtration, recombinant N-terminally His-tagged full-length MgtE from Escherichia coli strain C41 (DE3) by nickel affinity chromatography and gel filtration
recombinant periplasmic domain, glutathione S-transferase fusion protein
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Salmonella enterica EG13250 cells
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expression of HA-tagged wild-type and mutant enzymes in yeast
expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21, complementation of Salmonella typhimurium MM281, a strain devoid of all genomic Mg2+ transport systems
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expression of wild-type and mutant enzyme, the arginine rich motif of Mrs2p is not essential for the splicing of group II introns
gene corA, DNA and amino acid asequence determination
gene corA, DNA and amino acid sequence determination
gene mgtC is encoded in the pathogenicity island 3, SPI-3
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gene mgtE, expression in and functional complementation of a CorA Mg2+ transport mutant of Salmonella enterica serovar Thyphimurium
gene mgtE, overexpression of N-terminally His-tagged full-length enzyme and cytosolic domain in Escherichia coli strain C41 (DE3)
genes mgtA and mgtB, from complementation of the Mg2+ growth phenotype mutants MM7 and MM281, gene corA, DNA and amino acid sequence determination, the corA promoter does not respond to extracellular Mg2+ concentration, transcription factor PhoP is important in corA transcription regulation, overview
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is highly induced in the roots during Mg2+ deficiency
gene expression of the Mg2+ selective transporter MagT1 is upregulated in TRPM7-deficient cells. The enzyme level is elevated when cells are cultured in Mg2+ free medium for 24 h
overexpression of the Mg2+ transporter CorA decreases mgtA transcription
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Salmonella expresses the MgtA transporter only in Mg2+-depleted conditions. MgtA expression increases in a Salmonella strain lacking MgtR. The MgtR peptide is necessary for the MgtA protein to be induced at the normal timing upon Mg2+ starvation
the MgtR peptide limits levels of the MgtA protein at low Mg2+ concentrations
there is little mgtA transcription when strain YS802 is grown in media with more than 0.05 mM Mg2+, some transcription in 0.05 mM Mg2+, and maximum levels in 0.01 mM Mg2+
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C191A
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elimination of the only Cys residue of enzyme, mutant forms a tetramer like wild-type
L323A/L324A
mutation in potential basolateral sorting signal, does not affect basolateral localization of isoform CNNM4
L550A/L551A/L552A
mutation in potential basolateral sorting signal, does not affect basolateral localization of isoform CNNM4
L575A/L576A
mutation in potential basolateral sorting signal, mutant protein is expressed on both apical and basolateral surfaces in approximately half of the observed cells
L575A/L576A/L758A/L759A/L765A/L766A
mutation in potential basolateral sorting signals, mutant protein is found on both apical and basolateral surfaces in almost all of the observed cells. Mutation disrupts interaction with my1A and my1B
L578A/L579A
mutation in potential basolateral sorting signal, mutant vprotein is observed throughout the cytoplasm
L758A/L759A
mutation in potential basolateral sorting signal, mutant protein is expressed on both apical and basolateral surfaces in approximately half of the observed cells
L765A/L766A
mutation in potential basolateral sorting signal, mutant protein is expressed on both apical and basolateral surfaces in approximately half of the observed cells
Y351A
mutation in potential basolateral sorting signal, does not affect basolateral localization of isoform CNNM4
Y405A
mutation in potential basolateral sorting signal, does not affect basolateral localization of isoform CNNM4
Y488A
mutation in potential basolateral sorting signal, does not affect basolateral localization of isoform CNNM4
Y581A
mutation in potential basolateral sorting signal, does not affect basolateral localization of isoform CNNM4
Y708A
mutation in potential basolateral sorting signal, mutant vprotein is observed throughout the cytoplasm
D235R
loss-of-function mutation, site-directed mutagenesis, growth phenotype, overview
D244K
loss-of-function mutation, site-directed mutagenesis, growth phenotype, overview
E341D
site-directed mutagenesis, the substitution in the loop region of Mrs2p does not influence conductance of the Mg2+ channel
E341K
site-directed mutagenesis, the substitution in the loop region of Mrs2p abolish conductance of the Mg2+ channel
E342D
site-directed mutagenesis, the substitution in the loop region of Mrs2p does not influence conductance of the Mg2+ channel
E342K
site-directed mutagenesis, the substitution in the loop region of Mrs2p abolish conductance of the Mg2+ channel
M1301
gain-of-function mutation, random mutagenesis
R173E
loss-of-function mutation, site-directed mutagenesis, growth phenotype, overview
R768E
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isoform Alr2p, stimulation of Mg2+-transport activity of enzyme
E341D
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site-directed mutagenesis, the substitution in the loop region of Mrs2p does not influence conductance of the Mg2+ channel
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E341K
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site-directed mutagenesis, the substitution in the loop region of Mrs2p abolish conductance of the Mg2+ channel
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E342D
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site-directed mutagenesis, the substitution in the loop region of Mrs2p does not influence conductance of the Mg2+ channel
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E342K
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site-directed mutagenesis, the substitution in the loop region of Mrs2p abolish conductance of the Mg2+ channel
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C191S
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mutant retains function
C191S/C317
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addition of a Cys residue to enzyme cytoplasmic C-terminus, mutant retains function
E281A
the mutant shows no significant changes in apparent Mg2+ affinity
E281K/K287E
the apparent cation affinity of the double mutant is identical to that of wild type enzyme
E281L
the mutant shows no significant changes in apparent Mg2+ affinity
E281Q
the mutant shows no significant changes in apparent Mg2+ affinity
E281R
the mutant shows no significant changes in apparent Mg2+ affinity
E285A
non-functional mutant
E285D
non-functional mutant
E285K
non-functional mutant
E285Q
non-functional mutant
E285R
non-functional mutant
K287E
the mutation demonstrates a modest decrease in apparent Mg2+ affinity of 2-4fold, the mutation does not affect enzyme function significantly, although apparent Mg2+ affinity is decreased about 10fold
K287Q
the mutation does not affect enzyme function significantly, although apparent Mg2+ affinity is decreased about 10fold
K287R
the mutation does not affect enzyme function significantly, although apparent Mg2+ affinity is decreased about 10fold
M299C
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cross-linking in presence of Cu(II)-1,10-phenanthroline
S274C
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cross-linking in presence of Cu(II)-1,10-phenanthroline
T270C
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cross-linking in presence of Cu(II)-1,10-phenanthroline
Y292C
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cross-linking in presence of Cu(II)-1,10-phenanthroline and spontaneously
M299A
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mutant with decreased cation affinity
M299C
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mutant with decreased cation affinity
Y292C
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mutant with decreased transport properties
Y292F
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mutant with decreased transport properties
Y292I
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mutant with decreased transport properties
Y292S
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mutant with decreased transport properties
Y307A
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mutant with decreased cation affinity
Y307F
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mutant with decreased cation affinity
Y307S
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mutant with decreased cation affinity
D253F
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site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview
D253K
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site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview
D253W
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site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview
E206R
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site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview
E316K
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site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview
E316K/E320A
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site-directed mutagenesis, with mutation of Gly4alpha5alpha6, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview
E320K
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site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview
P303I
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site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview
V194E
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site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview
V194E/E206R
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site-directed mutagenesis, structural alterations and Mg2+ transport in comparison to the wild-type enzyme, overview
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
reconstitution of the purified recombinant enzyme in phosphatidylcholine liposomes, overview
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
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Overexpression of enzyme in Escherichia coli results in formation of inclusion bodies. Co-expression of DnaK/DnaJ prevents inclusion bodies and leads to the integration of more enzyme into the membrane. Co-expression of GroEL/GroES, Ffh/4.5S-RNA or SecA are less effective
medicine
synthesis
by overexpression of mgtA in Escherichia coli, a concentration of 32.41 g succinic acid per liter with a yield of 0.81 g per g glucose, can be obtained in a batch fermentation by using the low-cost mixture of Mg(OH)2 and NH3-H2O to replace MgCO3 as the alkaline neutralizer. The effect of the inhibitory compounds in lignocellulosic hydrolyzates on cell growth and succinic acid production can be relieved. In a 3-liter bioreactor, the overall productivity and yield of succinic acid in the whole anaerobic stage are 2.15 g per liter and h and 0.86 g per g total sugar, respectively
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