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D360A
mutation in labile copper coordination sphere, inactive
D360M
mutation at sites Cu5
D507A
about 10% increase in specific activity
D507N
about 80% increase in specific activity
E506A
mutation results in the formation of a compensatory hydrogen bond network with one or two extra water molecules
E506D
about 20% decrease in specific activity activity
E506I
mutation results in the complete shutdown of the hydrogen bond network leading to loss of enzymatic activities
E506Q
mutation results in the hydrogen bond network without the proton transport function
G304K
mutant shows markedly increased the laccase activity. Movements of the regulatory loop combined with the changes of the methionine-rich region may uncover the T1 Cu site allowing greater access of the substrate. Cuprous oxidase activity of mutant G304K is about 20% of wild-type activity, while the Km value is about 4times lower
M355L
mutation in labile copper coordination sphere, inactive
M355L/D360N
mutation at sites Cu5
M358S/M361S/M362S/M364S/M366S
mutation leads to an about 4fold reduction in kcat for Cu(I) oxidation
M358S/M361S/M362S/M368S/M376S
mutation leads to an about 4fold reduction in kcat for Cu(I) oxidation
M358S/M362S
mutation at sites Cu6
M358S/M362S/M364S/M368S
mutations at sites Cu6,7
M364S/M368S
mutation at sites Cu7
M441L
mutation in labile copper coordination sphere. Mutation has affected copper incorporation into the T1 copper site
M510L
3.8-4.2 copper atoms per protein molecule, similar to wild-type
M510Q
3.8-4.2 copper atoms per protein molecule, similar to wild-type
P444A/D439A
mutation leads to a synergetic effect of the positive shift in the redox potential of the type I copper center and the increase in enzyme activity
P444A/M510Q
3.4 copper atoms per protein molecule, similar to wild-type
P444G
mutation results in positive shifts in the redox potential of this copper center and enhanced oxidase activity in CueO and in the region Pro357-His406 deletion mutant lacking a methionine-rich helical segment that covers the substrate-binding site
P444I
positive shift in the redox potential of this copper center and enhanced oxidase activity
P444L
positive shift in the redox potential of this copper center and enhanced oxidase activity
C500S
-
mutation leads to loss of the T1 copper
-
M358S/M361S/M362S/M364S/M366S
-
mutation leads to an about 4fold reduction in kcat for Cu(I) oxidation
-
M455L
mutation in T1 Cu site, incorporation of 3-4 copper atoms, similar to wild-type. Mutation results in an increase of 100 mV in the O2 reduction potential, while the enzymatic activity for ABTS oxidation is decreased
M456A
mutation in T1 Cu site, incorporation of 3-4 copper atoms, similar to wild-type
C500S
mutant designed to incapacitate binding of the T1 copper, mutant protein does not support resistance to copper toxicity when placed in a cell line missing a functional CueO gene
C500S
mutation leads to loss of the T1 copper
D439A
3.8-4.2 copper atoms per protein molecule, similar to wild-type
D439A
mutation in labile copper coordination sphere, 3-4fold increase in Km value for Cu2+
D439A
positive shift in the redox potential of this copper center and enhanced oxidase activity
P444A
3.8-4.2 copper atoms per protein molecule, similar to wild-type
P444A
positive shift in the redox potential of this copper center and enhanced oxidase activity
additional information
deletion of the region Pro357-His406 comprising a methionine-rich helical segment that covers the substrate-binding site and replacement with a Gly-Gly linker. The scaffold of the CueO molecule and metal-binding sites are reserved in the mutant. The high thermostability of the protein molecule and its spectroscopic and magnetic properties are also conserved after truncation. The cuprous oxidase activity of the mutant is reduced to about 10% that of recombinant CueO due to the decrease in the affinity of the labile Cu site for Cu(I) ions
additional information
-
deletion of the region Pro357-His406 comprising a methionine-rich helical segment that covers the substrate-binding site and replacement with a Gly-Gly linker. The scaffold of the CueO molecule and metal-binding sites are reserved in the mutant. The high thermostability of the protein molecule and its spectroscopic and magnetic properties are also conserved after truncation. The cuprous oxidase activity of the mutant is reduced to about 10% that of recombinant CueO due to the decrease in the affinity of the labile Cu site for Cu(I) ions
additional information
mutations at Pro444 to construct a second NH-S hydrogen bond between the backbone amide and coordinating Cys500 thiolate of the type I copper result in positive shifts in the redox potential of this copper center and enhanced oxidase activity in CueO. Pro444 mutations limit the incorporation of copper ions into the trinuclear copper center. The activities of both CueO and the region Pro357-His406 deletion mutant are also enhanced by mutations to break down the hydrogen bond between the imidazole group of His443 that is coordinated to the type I copper and the beta-carboxy group of Asp439 that is located in the outer sphere of the type I copper center. The characteristics of the Cu(II)-S(Cys) bond are only minimally perturbed by mutations involving formation or disruption of a hydrogen bond from the coordinating groups to the type I copper
additional information
-
mutations at Pro444 to construct a second NH-S hydrogen bond between the backbone amide and coordinating Cys500 thiolate of the type I copper result in positive shifts in the redox potential of this copper center and enhanced oxidase activity in CueO. Pro444 mutations limit the incorporation of copper ions into the trinuclear copper center. The activities of both CueO and the region Pro357-His406 deletion mutant are also enhanced by mutations to break down the hydrogen bond between the imidazole group of His443 that is coordinated to the type I copper and the beta-carboxy group of Asp439 that is located in the outer sphere of the type I copper center. The characteristics of the Cu(II)-S(Cys) bond are only minimally perturbed by mutations involving formation or disruption of a hydrogen bond from the coordinating groups to the type I copper
additional information
-
deletion of the longest methionine-rich surface loop lowers bound extra Cu(I) from 9 in the wild-type enzyme to 2-3 Cu(I) in deletion mutants
additional information
-
deletion of the longest methionine-rich surface loop lowers bound extra Cu(I) from 9 in the wild-type enzyme to 2-3 Cu(I) in deletion mutants
-
additional information
-
truncated enzyme with a deleted methionine-rich C-terminal tail region shows a decreased turnover and a slightly lower Km value. Ki (Cu+) value increased compared to wild-type. Catalytic efficacy similar to wild-type
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Classen, T.; Pietruszka, J.; Schuback, S.M.
A new multicopper oxidase from Gram-positive bacterium Rhodococcus erythropolis with activity modulating methionine rich tail
Protein Expr. Purif.
89
97-108
2013
Rhodococcus erythropolis
brenda
Komori, H.; Kataoka, K.; Tanaka, S.; Matsuda, N.; Higuchi, Y.; Sakurai, T.
Exogenous acetate ion reaches the type II copper centre in CueO through the water-excretion channel and potentially affects the enzymatic activity
Acta Crystallogr. Sect. F
72
558-563
2016
Escherichia coli (P36649)
brenda
Grass, G.; Rensing, C.
CueO is a multi-copper oxidase that confers copper tolerance in Escherichia coli
Biochem. Biophys. Res. Commun.
286
902-908
2001
Escherichia coli (P36649)
brenda
Kajikawa, T.; Kataoka, K.; Sakurai, T.
Modifications on the hydrogen bond network by mutations of Escherichia coli copper efflux oxidase affect the process of proton transfer to dioxygen leading to alterations of enzymatic activities
Biochem. Biophys. Res. Commun.
422
152-156
2012
Escherichia coli (P36649), Escherichia coli
brenda
Kataoka, K.; Kogi, H.; Tsujimura, S.; Sakurai, T.
Modifications of laccase activities of copper efflux oxidase, CueO by synergistic mutations in the first and second coordination spheres of the type I copper center
Biochem. Biophys. Res. Commun.
431
393-397
2013
Escherichia coli (P36649), Escherichia coli
brenda
Kataoka, K.; Hirota, S.; Maeda, Y.; Kogi, H.; Shinohara, N.; Sekimoto, M.; Sakurai, T.
Enhancement of laccase activity through the construction and breakdown of a hydrogen bond at the type I copper center in Escherichia coli CueO and the deletion mutant Deltaalpha5-7 CueO
Biochemistry
50
558-565
2011
Escherichia coli (P36649), Escherichia coli
brenda
Clement, R.; Wang, X.; Biaso, F.; Ilbert, M.; Mazurenko, I.; Lojou, E.
Mutations in the coordination spheres of T1 Cu affect Cu2+-activation of the laccase from Thermus thermophilus
Biochimie
182
228-237
2021
Thermus thermophilus (Q72HW2), Thermus thermophilus
brenda
Roulling, F.; Godin, A.; Feller, G.
Function and versatile location of Met-rich inserts in blue oxidases involved in bacterial copper resistance
Biochimie
194
118-126
2022
Pseudoalteromonas haloplanktis, Pseudoalteromonas haloplanktis TAC125
brenda
Stoj, C.; Kosman, D.J.
Cuprous oxidase activity of yeast Fet3p and human ceruloplasmin implication for function
FEBS Lett.
554
422-426
2003
Homo sapiens (P00450), Homo sapiens, Saccharomyces cerevisiae (P38993), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (P38993)
brenda
Achard, M.E.; Tree, J.J.; Holden, J.A.; Simpfendorfer, K.R.; Wijburg, O.L.; Strugnell, R.A.; Schembri, M.A.; Sweet, M.J.; Jennings, M.P.; McEwan, A.G.
The multi-copper-ion oxidase CueO of Salmonella enterica serovar typhimurium is required for systemic virulence
Infect. Immun.
78
2312-2319
2010
Salmonella enterica subsp. enterica serovar Typhimurium (Q8ZRS2), Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 (Q8ZRS2)
brenda
Djoko, K.Y.; Chong, L.X.; Wedd, A.G.; Xiao, Z.
Reaction mechanisms of the multicopper oxidase CueO from Escherichia coli support its functional role as a cuprous oxidase
J. Am. Chem. Soc.
132
2005-2015
2010
Escherichia coli (P36649), Escherichia coli
brenda
Kim, C.; Lorenz, W.; Hoopes, J.; Dean, J.
Oxidation of phenolate siderophores by the multicopper oxidase encoded by the Escherichia coli yacK gene
J. Bacteriol.
183
4866-4875
2001
Escherichia coli (P36649)
brenda
Singh, S.K.; Grass, G.; Rensing, C.; Montfort, W.R.
Cuprous oxidase activity of CueO from Escherichia coli
J. Bacteriol.
186
7815-7817
2004
Escherichia coli (P36649), Escherichia coli
brenda
Outten, F.; Huffman, D.; Hale, J.; OHalloran, T.
The Independent cue and cus systems confer copper tolerance during aerobic and anaerobic growth in Escherichia coli
J. Biol. Chem.
276
30670-30677
2001
Escherichia coli (P36649)
brenda
Roberts, S.; Wildner, G.; Grass, G.; Weichsel, A.; Ambrus, A.; Rensing, C.; Montfort, W.
A labile regulatory copper ion lies near the T1 copper site in the multicopper oxidase CueO
J. Biol. Chem.
278
31958-31963
2003
Escherichia coli (P36649)
brenda
Singh, S.K.; Roberts, S.A.; McDevitt, S.F.; Weichsel, A.; Wildner, G.F.; Grass, G.B.; Rensing, C.; Montfort, W.R.
Crystal structures of multicopper oxidase CueO bound to copper(I) and silver(I) functional role of a methionine-rich sequence
J. Biol. Chem.
286
37849-3757
2011
Escherichia coli (P36649), Escherichia coli K12 (P36649)
brenda
Singh, S.K.; Roberts, S.A.; McDevitt, S.F.; Weichsel, A.; Wildner, G.F.; Grass, G.B.; Rensing, C.; Montfort, W.R.
Crystal structures of multicopper oxidase CueO bound to copper(I) and silver(I) functional role of a methionine-rich sequence
J. Biol. Chem.
286
37849-37857
2011
Escherichia coli (P36649)
brenda
Galli, I.; Musci, G.; Bonaccorsi Di Patti, M.
Sequential reconstitution of copper sites in the multicopper oxidase CueO
J. Biol. Inorg. Chem.
9
90-95
2004
Escherichia coli (P36649)
brenda
Kataoka, K.; Komori, H.; Ueki, Y.; Konno, Y.; Kamitaka, Y.; Kurose, S.; Tsujimura, S.; Higuchi, Y.; Kano, K.; Seo, D.; Sakurai, T.
Structure and function of the engineered multicopper oxidase CueO from Escherichia coli - deletion of the methionine-rich helical region covering the substrate-binding site
J. Mol. Biol.
373
141-152
2007
Escherichia coli (P36649), Escherichia coli
brenda
Cortes, L.; Wedd, A.G.; Xiao, Z.
The functional roles of the three copper sites associated with the methionine-rich insert in the multicopper oxidase CueO from E. coli
Metallomics
7
776-785
2015
Escherichia coli (P36649), Escherichia coli
brenda
Mancini, S.; Kumar, R.; Mishra, V.; Solioz, M.
Desulfovibrio DA2_CueO is a novel multicopper oxidase with cuprous, ferrous and phenol oxidase activity
Microbiology
163
1229-1236
2017
Desulfovibrio sp. A2 (G2H480)
brenda
Roberts, S.; Weichsel, A.; Grass, G.; Thakali, K.; Hazzard, J.; Tollin, G.; Rensing, C.; Montfort, W.
Crystal structure and electron transfer kinetics of CueO, a multicopper oxidase required for copper homeostasis in Escherichia coli
Proc. Natl. Acad. Sci. USA
99
2766-2771
2002
Escherichia coli (P36649)
brenda
Wang, H.; Liu, X.; Zhao, J.; Yue, Q.; Yan, Y.; Gao, Z.; Dong, Y.; Zhang, Z.; Fan, Y.; Tian, J.; Wu, N.; Gong, Y.
Crystal structures of multicopper oxidase CueO G304K mutant structural basis of the increased laccase activity
Sci. Rep.
8
14252
2018
Escherichia coli (P36649), Escherichia coli
brenda