Information on EC 3.6.3.54 - Cu+-exporting ATPase

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

EC NUMBER
COMMENTARY hide
3.6.3.54
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RECOMMENDED NAME
GeneOntology No.
Cu+-exporting ATPase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + Cu+[side 1] = ADP + phosphate + Cu+[side 2]
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (Cu+-exporting)
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme transports Cu+ or Ag+, and cannot transport the divalent ions, contrary to EC 3.6.3.4, Cu2+-exporting ATPase, which mainly transports the divalent copper ion.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
gene cutP
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-
Manually annotated by BRENDA team
gene cutP
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-
Manually annotated by BRENDA team
gene Tgcutp
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
physiological function
additional information
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 + Ag+[side 1]
ADP + phosphate + Ag+[side 2]
show the reaction diagram
ATP + H2O + Cu+
ADP + phosphate + Cu+
show the reaction diagram
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-
-
-
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ATP + H2O + Cu+[side 1]
ADP + phosphate + Cu+[side 2]
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 + Cu+
ADP + phosphate + Cu+
show the reaction diagram
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-
-
-
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ATP + H2O + Cu+[side 1]
ADP + phosphate + Cu+[side 2]
show the reaction diagram
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Sodium azide
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inhibits ATP hydrolysis
vanadate
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inhibitor
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Bathocuproine disulfonate
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i.e. BCS, Cu(I) chelator, reduces enzyme activity
hydroxylamine
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sensitive to
KOH
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sensitive to
N,N-Dimethyldodecylamine-N-oxide
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N-methylglucamine
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n-octyl beta-D-glucopyranoside
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additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cys
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millimolar concentration of Cys increase the activity about 800fold. Cys is a non-essential activator of the enzyme, interacting with the cytoplasmic side of the enzyme. K1/2 of 4 mM
L-cysteine
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isoform CtrA2 shows highest activity at 20 mM L-cysteine, isoform CtrA3 shows highest activity at 15 mM L-cysteine
NaCl
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highest activity at about 400 mM NaCl
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.22 - 0.5
ATP
0.00045 - 0.0015
Cu+
0.0031
Cu+[side 1]
at pH 6.0 and 60°C
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0047
oligomycin
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pH 6.1, 75°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
25
N-methylglucamine
Archaeoglobus fulgidus
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pH 6.1, 75°C
0.024
vanadate
Archaeoglobus fulgidus
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pH 6.1, 75°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
ATPase hydrolysis rates of purified and reconstituted wild-type CopA and enzyme truncation mutants
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
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assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7
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pH 6.0: about 30% of maximal activity, pH 7.0: about 30% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
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assay at room temperature
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60 - 80
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60°C: about 55% of maximal activity, 80°C: about 75% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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Cu-regulated localization in hepatocytes
Manually annotated by BRENDA team
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high Cu2+ concentration redistributes ATP7B to late endosomes or lysosomes that move along the axon in live hippocampal neurons
Manually annotated by BRENDA team
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enzyme ATP7B is localized to the trans-Golgi network and the plasma membrane of the soma and dendrites but not the axon. Addition of high Cu2+ concentrations cause loss of somatodendritic polarity of ATP7B. High Cu2+ concentration redistributes ATP7B to late endosomes or lysosomes that move along the axon in live hippocampal neurons
Manually annotated by BRENDA team
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Cu levels regulate the reversible trafficking of endogenous ATP7B in polarized WIF-B cells
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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luminal acidification is required for the cell to redirect ATP7B to the apical domain and maintain it there under conditions of high Cu. Deacidification prevents Cu-directed delivery to apical domain
Manually annotated by BRENDA team
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high Cu2+ concentration redistributes ATP7B to late endosomes or lysosomes that move along the axon in live hippocampal neurons
Manually annotated by BRENDA team
additional information
PDB
SCOP
CATH
ORGANISM
UNIPROT
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Synechocystis sp. (strain PCC 6803 / Kazusa)
Synechocystis sp. (strain PCC 6803 / Kazusa)
Synechocystis sp. (strain PCC 6803 / Kazusa)
Synechocystis sp. (strain PCC 6803 / Kazusa)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
78000
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x * 78000, isoform CtrA3, SDS-PAGE
80000
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x * 80000, isoform CtrA2, SDS-PAGE
83300
x * 83300, SELDI-TOF mass spectrometry
150000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting drop method, crystal structure of the apo, oxidized C-terminal-metal binding domain to 2.0 A resolution. In the structure, two C-terminal-metal binding domain monomers form a domain-swapped dimer
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wild-type and selenomethionine CopA-ATP binding domain, hanging drop vapor diffusion method, using 100 mM sodium acetate, pH 4.6, 5–8% polyethylene glycol 4000, and 10–20% glycerol
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with bound adenosine 5'-[beta, gamma-methylene]triphosphate or ADP and Mg2+, vapor diffusion method, using 5% (w/v) PEG 6000, 1.25-1.5M NaCl and 100 mM MES, pH 5.5-5.75, at 10°C
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structure determination of the 73-147 domain in the 1-151 construct, in the apo state through 1H, 15N and 13C NMR spectroscopies, the structure of the Cu(I)-loaded 73-147 domain has been also determined in the construct 73-151
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
66 - 85
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incubation of CopA in the absence of substrates at temperatures in the 66–85°C range leads to an irreversible exponential decrease in enzyme activity suggesting a two-state process involving fully-active and inactive molecules. Although CopA inactivated much slower than mesophilic proteins, the activation energy is similar to that observed for mesophilic P-type ATPases. The inactivation process is found to be associated with the irreversible partial unfolding of the polypeptide chain. However, the inactive thermally denatured protein still conserves large hydrophobic regions and considerable secondary structure
75
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complete and irreversible inactivation after 70 min
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
guanidine-HCl
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the incubation of the enzyme reconstituted in phospholipid/detergent mixed micelles with high concentrations of guanidinium hydrochloride at 25°C induces a reversible decrease in fluorescence quantum yield, far-UV ellipticity, and loss of ATPase and phosphatase activities. Refolding of the enzyme from this unfolded state leads to recovery of full biological activity and all the structural features of the native enzyme. The unfolding shows typical characteristics of a two-state process. Most of the secondary and tertiary structures are disrupted. The fraction of Trp fluorescence accessible to soluble quenchers shifts from 0.52 in the native state to 0.96 in the unfolded state, with a significant spectral redshift. Hydrophobic patches in the enzyme, mainly located in the transmembrane region, are disrupted as indicated by 1-anilino-naphtalene-8-sulfonate fluorescence. Nevertheless, the unfolded state has a small but detectable amount of residual structure, which might play a key role in both CopA folding and adaptation for working at high temperatures
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; Ni-NTA column chromatography
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Co2+ metal affinity resin column chromatography, and gel filtration
CopA purified from dodecylmaltoside-solubilized membranes by metal chelate affinity chromatography, presence of a small amount of copper during solubilization and purification found to result in a more active and stable CopA
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gene copAab, recombinant full-length enzyme and N-terminal domains CopAa and CopAb from Escherichia coli strain BL21(DE3) by anion exchange chromatography, ultrafiltration, and gel filtration
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Ni Sepharose 6 column chromatography and Superdex 75 gel filtration
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Ni2+-NTA column chromatography
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recombinant His-tagged MBP-fusion enzyme from Escherichia coli by nickel affinity chromatography and gel filtration
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streptactin column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
CopA cDNA lacking the N-terminal metal binding domain and the C-terminal metal-binding domain coding regions is ligated into pEXP-NT vector, which adds an N terminus His6 tag sequence is used as a template to introduce the mutations coding for the single substitutions M158A, M158C, E205A, E205C, D336A, and D336C, and the multiple replacements S139A/G140A and K145A/S149A/R152A/R153A/R154A; expressed in Escherichia coli BL21(DE3) cells
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enzyme overexpression in transgenic mmice
expressed in COS-1 cells
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expressed in Escherichia coli
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3)pLysS cells; expression in Escherichia coli
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expressed in Escherichia coli BL21Star(DE3)pLysS cells
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expressed in Escherichia coli DC194 cells
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expressed in Escherichia coli DH5alpha cells
expressed in Escherichia coli Top10 cells
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gene copA lacking the N-metal-binding-domain-coding regions, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)lambda
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gene copA, phylogenetic analysis and sequence comparisons, recombinant expression of Sulfolobus solfataricus CopA in Escherichia coli strain DC194, deficient in the PIB-type copper export ATPase copA, yielding poor or partial complementation; gene copB, phylogenetic analysis and sequence comparisons, recombinant expression of Sulfolobus solfataricus CopB in Escherichia coli strain DC194, deficient in the PIB-type copper export ATPase copA, yielding poor or partial complementation
gene copAab, expression of full-length enzyme and N-terminal domains CopAa and CopAb in Escherichia coli strain BL21(DE3)
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gene Tgcutp or TGGT1_020170, recombinant expression of the Myc2-tagged enzyme in Toxoplasma gondii
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microsomes derived from COS-1 cells infected with adenovirus vector and expressing recombinant ATP7A/B
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Recombinant adenovirus vector, rAdATP7Bmyc, containing CMV promoter driven WT human ATP7B cDNA, fused with 30 cmyc tag, expression in COS-1 cells
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recombinant expression in rat intestinal epithelial IEC-6 cells, Atp7a protein expression is induced more strongly than mRNA in the duodenum of iron-deprived rats, real-time quantitative RT-PCR enzyme expression analysis
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recombinant expression of His-tagged MBP-fusion enzyme in Escherichia coli, overexpression of GFP-tagged ATP7B in Rattus norvegicus hippocampal neurons, co-expression with myc-tagged wild-type or V98S-mutant sigma1A, with HA-tagged wild-type or V98S-mutant sigma1B, and with HA-tagged wild-type or V98S-mutant sigma1C
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recombinant expression of the N-terminal domain of human ATP7B (N-ATP7B) fused to maltose-binding protein, and FLAG-tagged enzyme in HEK293T-Rex cells, co-expression of GFP-tagged nanoparticle in HEK-293T cells, the nanobodies bind to the distinct regions of N-ATP7B, binding sites of 2R50 and 2R51 are located within metal binding domains MBD1-4, revealing transient inter-domain interactions in N-ATP7B
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the N-terminal region of BsCopA contains two domains constituted by amino acid residues 1 to 72 and 73 to 147, which are expressed both separately and together, in both cases only the 73-147 domain is folded and is stable both in the copper(I)-free and in the copper(I)-bound forms
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
an increase in the external copper concentration induces the enzyme; an increase in the external copper concentration induces the enzyme
Atp7a expression is upregulated by iron chelation and copper loading. Recombinant Atp7a protein expression is induced more strongly than mRNA in the duodenum of iron-deprived rats, Atp7a expression is upregulated by iron chelation and copper loading, iron chelation increases Atp7a mRNA expression by 1.6fold, but has little effect on protein levels
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copper has a direct influence on Atp7a protein expression independent of changes in mRNA levels
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copper transporter ATP7A protein expression is significantly reduced in blood vessels from type 1 diabetes mellitus mice
insulin treatment, but not high glucose, increases enzyme ATP7A expression in vascular smooth muscles cells
Sulfolobus responds to exposure to a sublethal copper excess by the transient active transcription of the copA gene. The copA transcript reaches a peak 1 h after treatment, corresponding to approximately 35fold the uninduced level. Thereafter, the transcript level decreases until a steady-state level of 2-3fold induction is reached in the following 16 h. In cells cultured for several generations in the presence of 0.75 mM copper, the amount of copA transcript is maintained at 2-3fold the uninduced level, indicating that its rate of expression is maintained constant during longterm exposures, provided the concentration of copper do not change
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Sulfolobus responds to exposure to a sublethal copper excess by the transient active transcription of the copA gene. The copA transcript reaches a peak 1 h after treatment, corresponding to approximately 35fold the uninduced level. Thereafter, the transcript level decreases until a steady-state level of 2-3fold induction is reached in the following 16 h. In cells cultured for several generations in the presence of 0.75 mM copper, the amount of copA transcript is maintained at 2-3fold the uninduced level, indicating that its rate of expression is maintained constant during longterm exposures, provided the concentration of copper do not change; the copA gene is expressed at basal levels in untreated cells of both strain PBL2025 and strain PBL2050. After copper stress, the level of copA transcript increases approximately 30fold. The gene Sso2652 (copR) of the Sulfolobus solfataricus genome encodes a transcriptional activator of the copper-transporting ATPase CopA gene. The CopR protein is a copper-responsive regulators
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the copA gene is expressed at basal levels in untreated cells of both strain PBL2025 and strain PBL2050. After copper stress, the level of copA transcript increases approximately 30fold. The gene Sso2652 (copR) of the Sulfolobus solfataricus genome encodes a transcriptional activator of the copper-transporting ATPase CopA gene. The CopR protein is a copper-responsive regulators
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C27A/C30A
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replacement of Cys in the N-terminal metal binding domain, mutation leads to about 40% reduction in Ag+ activated ATPase activity and about 60% reduction in Cu+-activated ATPase activity. The mutant enzyme binds Cu+, Ag+, and ATP with the same high apparent affinities as the wild-type enzyme. Evidence that the N-terminal metal binding domain disruption has no effect on the E1-E2 equilibrium is provided by the normal interaction of ATP acting with low affinity and the unaffected IC50 for vanadate inhibition observed in the C27A/C30A-substituted enzyme
C27A/C30A/C751A/C754A
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mutation leads to about 40% reduction in Ag+ activated ATPase activity and about 60% reduction in Cu+-activated ATPase activity
C380A/C382A
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the mutant enzyme binds ATP, indicating its correct folding and suggesting that enzyme turnover is prevented by the lack of metal binding to the transmembrane site
C382A
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the mutant exhibits reduced copper binding activity
C751A/C754A
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the mutant enzyme has no significant effect on ATPase activity, enzyme phosphorylation, apparent binding affinities of ligands, or E1-E2 equilibrium
D336A
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free Cu+/ATPase activity kinetic parameters and binding stoichiometry of wild type and mutant enzyme; mutation does not affect the ATPase activity when stimulated by free Cu+ in the assay media, nor does the mutation impair Cu+ binding to transmembrane metal-binding site; the mutant shows increased Vmax value compared to the wild type enzyme
D336C
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free Cu+/ATPase activity kinetic parameters and binding stoichiometry of wild type and mutant enzyme; mutation does not affect the ATPase activity when stimulated by free Cu+ in the assay media, nor does the mutation impair Cu+ binding to transmembrane metal-binding site; the mutant shows increased Vmax value compared to the wild type enzyme
E205A
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free Cu+/ATPase activity kinetic parameters and binding stoichiometry of wild type and mutant enzyme; mutation does not affect the ATPase activity when stimulated by free Cu+ in the assay media, nor does the mutation impair Cu+ binding to transmembrane metal-binding site; the mutant shows increased Vmax value compared to the wild type enzyme
E205C
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free Cu+/ATPase activity kinetic parameters and binding stoichiometry of wild type and mutant enzyme; mutation does not affect the ATPase activity when stimulated by free Cu+ in the assay media, nor does the mutation impair Cu+ binding to transmembrane metal-binding site; the mutant shows increased Vmax value compared to the wild type enzyme
H462Q
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the mutation reduces the affinity for adenosine 5'-[beta, gamma-methylene]triphosphate about 20fold
I685E
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Cu+/ATPase activity is about 50% of the activity of the wild-type enzyme
I685T
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Cu+/ATPase activity is about 25% of the activity of the wild-type enzyme
K145A/S149A/R152A/R153A/R154A
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mutation does not affect the ATPase activity when stimulated by free Cu+ in the assay media, nor does the mutation impair Cu+ binding to transmembrane metal-binding site
L686A
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Cu+/ATPase activity is about 80% of the activity of the wild-type enzyme
M158A
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free Cu+/ATPase activity kinetic parameters and binding stoichiometry of wild type and mutant enzyme; mutation does not affect the ATPase activity when stimulated by free Cu+ in the assay media, nor does the mutation impair Cu+ binding to transmembrane metal-binding site; the mutant shows reduced Vmax value compared to the wild type enzyme
M158C
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free Cu+/ATPase activity kinetic parameters and binding stoichiometry of wild type and mutant enzyme; mutation does not affect the ATPase activity when stimulated by free Cu+ in the assay media, nor does the mutation impair Cu+ binding to transmembrane metal-binding site; the mutant shows increased Vmax value compared to the wild type enzyme
M711C
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no Cu+/ATPase activity
N683A
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no Cu+/ATPase activity
N683Q
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no Cu+/ATPase activity
P688A
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Cu+/ATPase activity is about 70% of the activity of the wild-type enzyme
P704A
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Cu+/ATPase activity is about 75% of the activity of the wild-type enzyme
S139A/G140A
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free Cu+/ATPase activity kinetic parameters and binding stoichiometry of wild type and mutant enzyme; mutation does not affect the ATPase activity when stimulated by free Cu+ in the assay media, nor does the mutation impair Cu+ binding to transmembrane metal-binding site; the mutant shows increased Vmax value compared to the wild type enzyme
S714A
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Cu+/ATPase activity is about 30% of the activity of the wild-type enzyme
S714R
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Cu+/ATPase activity is about 65% of the activity of the wild-type enzyme
S715R
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no Cu+/ATPase activity
Y682S
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Cu+/ATPase activity is about 10% of the activity of the wild-type enzyme
C14A/C17A/C110A/C113A
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increase in affinity for Cu(II)
C14S/C17S
site-directed mutagenesis, a dysfunctional non-copper-binding mutant
C479A
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mutation results in lost of resistance to copper
C481A
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mutation results in lost of resistance to copper
C481H
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mutation results in lost of resistance to copper
D207A/N208A/M209A/M210A
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site-directed mutagenesis
E287A
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site-directed mutagenesis
E287C
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site-directed mutagenesis
K23A/K30A/K31A/H35A/R50A
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site-directed mutagenesis
M204A
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site-directed mutagenesis
M204C
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site-directed mutagenesis
M279A/E280A/H283A
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site-directed mutagenesis
T212A/D214A/N215A/S217A
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site-directed mutagenesis
W273A/W276A/F277A
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site-directed mutagenesis
W797A/T800A/T802A
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site-directed mutagenesis
C575A/C578A
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mutation in the 6th copper site of the NMBD, catalytically inactive, no phosphoenzyme intermediate formed upon addition of ATP
C983A/C985A
D1027N
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the mutant is less phosphorylated than the wild type enzyme
H479Q
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the mutant is unable to utilize ATP, whereas phosphorylation by phosphate is retained
additional information
Show AA Sequence (680 entries)
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