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0.5
-
amidase activity wild-type Helicobacter pylori 26695, pH 7.0, 500 micromol NiCl2 supplementation
0.55
-
amidase activity wild-type Helicobacter pylori 26695, pH 7.0, 1000 micromol NiCl2 supplementation
0.6
-
amidase activity wild-type Helicobacter pylori 26695, pH 5.5
2.73
purified recombinant formamidase
20
-
urease activity wild-type Helicobacter pylori 26695, pH 5.5
25
-
formamidase activity wild-type Helicobacter pylori 26695, pH 5.5
30
-
urease activity wild-type Helicobacter pylori 26695, pH 7.0, 1 micromol NiCl2 supplementation
5.2
-
formamidase activity wild-type Helicobacter pylori 26695, pH 7.0, 1000 micromol NiCl2 supplementation
60
-
urease activity wild-type Helicobacter pylori 26695, pH 7.0, 100 micromol NiCl2 supplementation
70
-
urease activity wild-type Helicobacter pylori 26695, pH 7.0, 1000 micromol NiCl2 supplementation
75
-
urease activity wild-type Helicobacter pylori 26695, pH 7.0, 500 micromol NiCl2 supplementation
8.1
-
formamidase activity wild-type Helicobacter pylori 26695, pH 7.0, 100 micromol NiCl2 supplementation
0.05
-
amidase activity wild-type Helicobacter pylori 26695, pH 7.0, 0 micromol NiCl2 supplementation
0.05
-
amidase activity wild-type Helicobacter pylori 26695, pH 7.0, 1 micromol NiCl2 supplementation
0.1
-
amidase activity wild-type Helicobacter pylori 26695, pH 7.0
0.1
-
amidase activity wild-type Helicobacter pylori 26695, pH 7.0, 100 micromol NiCl2 supplementation
5
-
formamidase activity wild-type Helicobacter pylori 26695, pH 7.0
5
-
urease activity wild-type Helicobacter pylori 26695, pH 7.0
6
-
formamidase activity wild-type Helicobacter pylori 26695, pH 7.0, 0 micromol NiCl2 supplementation
6
-
formamidase activity wild-type Helicobacter pylori 26695, pH 7.0, 1 micromol NiCl2 supplementation
8
-
formamidase activity wild-type Helicobacter pylori 26695, pH 7.0, 500 micromol NiCl2 supplementation
8
-
urease activity wild-type Helicobacter pylori 26695, pH 7.0, 0 micromol NiCl2 supplementation
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evolution
the enzyme is a nitrilase superfamily member
evolution
the enzyme is a nitrilase superfamily member
evolution
-
the enzyme is a nitrilase superfamily member
-
evolution
-
the enzyme is a nitrilase superfamily member
-
evolution
-
the enzyme is a nitrilase superfamily member
-
evolution
-
the enzyme is a nitrilase superfamily member
-
evolution
-
the enzyme is a nitrilase superfamily member
-
evolution
-
the enzyme is a nitrilase superfamily member
-
evolution
-
the enzyme is a nitrilase superfamily member
-
evolution
-
the enzyme is a nitrilase superfamily member
-
evolution
-
the enzyme is a nitrilase superfamily member
-
additional information
a cysteine carbamoyl-switch is responsible for the inhibition of formamidase. Structure comparisons of Bacillus cereus AmiF and HpyAmiF
additional information
-
a cysteine carbamoyl-switch is responsible for the inhibition of formamidase. Structure comparisons of Bacillus cereus AmiF and HpyAmiF
additional information
a cysteine carbamoyl-switch is responsible for the inhibition of formamidase. Structure comparisons of BceAmiF and Helicobacter pylori AmiF
additional information
-
a cysteine carbamoyl-switch is responsible for the inhibition of formamidase. Structure comparisons of BceAmiF and Helicobacter pylori AmiF
additional information
-
a cysteine carbamoyl-switch is responsible for the inhibition of formamidase. Structure comparisons of BceAmiF and Helicobacter pylori AmiF
-
additional information
-
a cysteine carbamoyl-switch is responsible for the inhibition of formamidase. Structure comparisons of BceAmiF and Helicobacter pylori AmiF
-
additional information
-
a cysteine carbamoyl-switch is responsible for the inhibition of formamidase. Structure comparisons of BceAmiF and Helicobacter pylori AmiF
-
additional information
-
a cysteine carbamoyl-switch is responsible for the inhibition of formamidase. Structure comparisons of BceAmiF and Helicobacter pylori AmiF
-
additional information
-
a cysteine carbamoyl-switch is responsible for the inhibition of formamidase. Structure comparisons of BceAmiF and Helicobacter pylori AmiF
-
additional information
-
a cysteine carbamoyl-switch is responsible for the inhibition of formamidase. Structure comparisons of Bacillus cereus AmiF and HpyAmiF
-
additional information
-
a cysteine carbamoyl-switch is responsible for the inhibition of formamidase. Structure comparisons of BceAmiF and Helicobacter pylori AmiF
-
additional information
-
a cysteine carbamoyl-switch is responsible for the inhibition of formamidase. Structure comparisons of Bacillus cereus AmiF and HpyAmiF
-
additional information
-
a cysteine carbamoyl-switch is responsible for the inhibition of formamidase. Structure comparisons of BceAmiF and Helicobacter pylori AmiF
-
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dimer
-
alpha2, 2 * 51000, SDS-PAGE
trimer
-
3 * 44481, electrospray mass spectrometry
homotetramer
-
4 * 38000, His-tagged enzyme, SDS-PAGE
homotetramer
-
4 * 38632, His-tagged enzyme, calculated from amino acid sequence
homotetramer
-
4 * 38000, His-tagged enzyme, SDS-PAGE
-
homotetramer
-
4 * 38632, His-tagged enzyme, calculated from amino acid sequence
-
homotetramer
4 * 32000, calculated from amino acid sequence
homotetramer
-
4 * 3400, SDS-PAGE, 4 * 37300, deduced from gene sequence
homotetramer
4 * 45000, SDS-PAGE
homotetramer
4 * 43300, native state, native PAGE
additional information
enzyme structure analysis by dynamic light scattering, circular dichroism, gel filtration, and mass spectrometry
additional information
-
enzyme structure analysis by dynamic light scattering, circular dichroism, gel filtration, and mass spectrometry
additional information
-
enzyme structure analysis by dynamic light scattering, circular dichroism, gel filtration, and mass spectrometry
-
additional information
-
enzyme structure analysis by dynamic light scattering, circular dichroism, gel filtration, and mass spectrometry
-
additional information
-
enzyme structure analysis by dynamic light scattering, circular dichroism, gel filtration, and mass spectrometry
-
additional information
-
enzyme structure analysis by dynamic light scattering, circular dichroism, gel filtration, and mass spectrometry
-
additional information
-
enzyme structure analysis by dynamic light scattering, circular dichroism, gel filtration, and mass spectrometry
-
additional information
-
enzyme structure analysis by dynamic light scattering, circular dichroism, gel filtration, and mass spectrometry
-
additional information
-
enzyme structure analysis by dynamic light scattering, circular dichroism, gel filtration, and mass spectrometry
-
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E140D
-
the mutation does not significantly alter enzyme folding and shows no detectable activity
W136H
-
this mutation causes the absence of overexpression of the enzyme
Y191F
-
the mutation does not significantly alter enzyme folding and shows 11.8% activity compared to the wild type enzyme
E140D
-
the mutation does not significantly alter enzyme folding and shows no detectable activity
-
W136H
-
this mutation causes the absence of overexpression of the enzyme
-
Y191F
-
the mutation does not significantly alter enzyme folding and shows 11.8% activity compared to the wild type enzyme
-
SeMet-substituted form
MAD data collection
C166A
-
no enzymic activity
C166S
-
no enzymic activity
fur mutant
-
amidase activity at pH 5.5: wild-type 0.6, mutant 3.0 - at pH 7.0: wild-type 0.1, mutant 2.9
fur mutant
-
formamidase activity at pH 5.5: wild-type 25, mutant 41 - at pH 7.0: wild-type 5, mutant 41
fur mutant
-
urease activity at pH 5.5: wild-type 20, mutant 23 - at pH 7.0: wild-type 4, mutant 3
nikR fur double mutant
-
amidase activity at pH 5.5: wild-type 0.6, mutant 1.9 - at pH 7.0: wild-type 0.1, mutant 3.0
nikR fur double mutant
-
formamidase activity at pH 5.5: wild-type 25, mutant 30 - at pH 7.0: wild-type 5, mutant 40
nikR fur double mutant
-
urease activity at pH 5.5: wild-type 20, mutant 14 - at pH 7.0: wild-type 4, mutant 6
nikR mutant
-
amidase activity at pH 5.5: wild-type 0.6, mutant 0.2 - at pH 7.0: wild-type 0.1, mutant 0.1
nikR mutant
-
formamidase activity at pH 5.5: wild-type 25, mutant 8 - at pH 7.0: wild-type 5, mutant 5
nikR mutant
-
urease activity at pH 5.5: wild-type 20, mutant 13 - at pH 7.0: wild-type 4, mutant 5
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Mills, J.; Greenwood, J.A.; Jones, C.W.
The effect of growth in continuous culture at various input C:N ratios on the expression of proteins involved in the transport and metabolism of methanol and short-chain amides by Methylophilus methylotrophus
FEMS Microbiol. Lett.
161
173-178
1998
Methylophilus methylotrophus
-
brenda
Skouloubris, S.; Labigne, A.; de Reuse H.
Identification and characterization of an aliphatic amidase in Helicobacter pylori
Mol. Microbiol.
25
989-998
1997
Helicobacter pylori
brenda
Wyborn, N.R.; Mills, J.; Williams, S.G.; Jones, C.W.
Molecular characterization of formamidase from Methylophilus methylotrophus
Eur. J. Biochem.
240
314-322
1996
Methylophilus methylotrophus
brenda
Wyborn N.R.; Scherr, D.J.; Jones, C.W.
Purification, properties and heterologous expression of formamidase from Methylophilus methylotrophus
Microbiology
140
191-195
1994
Methylophilus methylotrophus
-
brenda
Friedrich, C.G.; Mitrenga, G.
Utilization of aliphatic amides and formation of two different amidases by Alcaligenes eutrophus
J. Gen. Microbiol.
125
367-374
1981
Cupriavidus necator
-
brenda
Magalhaes, M.; Campos, G.; Almeida, T.
Formidase activity in mycobacteria
Rev. Microbiol.
3
45-46
1972
Mycolicibacterium fortuitum
-
brenda
Clarke, P.H.
The aliphatic amidases of Pseudomonas aeruginosa
Adv. Microb. Physiol.
4
179-222
1970
Mycolicibacterium phlei, Mycolicibacterium smegmatis, Pseudomonas aeruginosa, Pseudomonas aeruginosa 8602
-
brenda
Skouloubris, S.; Labigne, A.; de Reuse H.
The AmiE aliphatic amidase and AmiF formamidase of Helicobacter pylori: natural evolution of two enzyme paralogues
Mol. Microbiol.
40
596-609
2001
Helicobacter pylori
brenda
Wu, G.; Huang, Q.; Tang, Y.; Unno, H.; Kusunoki, M.
Crystallization and preliminary crystallographic study of a recombinant predicted acetamidase/formamidase from the thermophile Thermoanaerobacter tengcongensis
Acta Crystallogr. Sect. F
F61
106-108
2005
Caldanaerobacter subterraneus subsp. tengcongensis (Q8R8S5), Caldanaerobacter subterraneus subsp. tengcongensis
brenda
van Vliet, A.H.; Kuipers, E.J.; Stoof, J.; Poppelaars, S.W.; Kusters, J.G.
Acid-responsive gene induction of ammonia-producing enzymes in Helicobacter pylori is mediated via a metal-responsive repressor cascade
Infect. Immun.
72
766-773
2004
Helicobacter pylori
brenda
Borges, C.L.; Pereira, M.; Felipe, M.S.; de Faria, F.P.; Gomez, F.J.; Deepe, G.S.; Soares, C.M.
The antigenic and catalytically active formamidase of Paracoccidioides brasiliensis: protein characterization, cDNA and gene cloning, heterologous expression and functional analysis of the recombinant protein
Microbes Infect.
7
66-77
2005
Paracoccidioides brasiliensis (Q8J0S3), Paracoccidioides brasiliensis
brenda
Hung, C.L.; Liu, J.H.; Chiu, W.C.; Huang, S.W.; Hwang, J.K.; Wang, W.C.
Crystal structure of Helicobacter pylori formamidase AmiF reveals a cysteine-glutamate-lysine catalytic triad
J. Biol. Chem.
282
12220-12229
2007
Helicobacter pylori
brenda
Han, W.; Zhou, Y.; Luo, Q.; Yao, Y.; Li, Z.
On the 3D structure and catalytic mechanism study of AmiF formamidase of Helicobacter pylori
Polymer
48
3726-3731
2007
Helicobacter pylori (O25836)
-
brenda
Borges, C.L.; Parente, J.A.; Barbosa, M.S.; Santana, J.M.; Bao, S.N.; de Sousa, M.V.; de Almeida Soares, C.M.
Detection of a homotetrameric structure and protein-protein interactions of Paracoccidioides brasiliensis formamidase lead to new functional insights
FEMS Yeast Res.
10
104-113
2010
Paracoccidioides brasiliensis (C1GWV9), Paracoccidioides brasiliensis
brenda
Rath, M.; Salas, J.; Parhy, B.; Norton, R.; Menakuru, H.; Sommerhalter, M.; Hatlstad, G.; Kwon, J.; Allan, D.; Vance, C.; Uhde-Stone, C.
Identification of genes induced in proteoid roots of white lupin under nitrogen and phosphorus deprivation, with functional characterization of a formamidase
Plant Soil
334
137-150
2010
Lupinus albus (B9VXW6)
-
brenda
Soriano-Maldonado, P.; Martinez-Gomez, A.I.; Andujar-Sanchez, M.; Neira, J.L.; Clemente-Jimenez, J.M.; Las Heras-Vazquez, F.J.; Rodriguez-Vico, F.; Martinez-Rodriguez, S.
Biochemical and mutational studies of the Bacillus cereus CECT 5050T formamidase support the existence of a C-E-E-K tetrad in several members of the nitrilase superfamily
Appl. Environ. Microbiol.
77
5761-5769
2011
Bacillus cereus, Bacillus cereus CECT 5050T
brenda
Qian, M.; Huang, Q.; Wu, G.; Lai, L.; Tang, Y.; Pei, J.; Kusunoki, M.
Crystal structure analysis of a recombinant predicted acetamidase/formamidase from the thermophile Thermoanaerobacter tengcongensis
Protein J.
31
166-174
2012
Caldanaerobacter subterraneus subsp. tengcongensis (Q8R8S5), Caldanaerobacter subterraneus subsp. tengcongensis
brenda
Martinez-Rodriguez, S.; Conejero-Muriel, M.; Gavira, J.A.
A novel cysteine carbamoyl-switch is responsible for the inhibition of formamidase, a nitrilase superfamily member
Arch. Biochem. Biophys.
662
151-159
2019
Helicobacter pylori (O25836), Helicobacter pylori, Bacillus cereus (P59701), Bacillus cereus, Bacillus cereus ATCC 14579 (P59701), Bacillus cereus NRRL B-3711 (P59701), Bacillus cereus NCIMB 9373 (P59701), Bacillus cereus CECT 148 (P59701), Bacillus cereus DSM 31 (P59701), Helicobacter pylori ATCC 700392 (O25836), Bacillus cereus NBRC 15305 (P59701), Helicobacter pylori 26695 (O25836), Bacillus cereus JCM 2152 (P59701)
brenda