BRENDA - Enzyme Database show
show all sequences of 1.7.1.13

Protection of the queuosine biosynthesis enzyme QueF from irreversible oxidation by a conserved intramolecular disulfide

Mohammad, A.; Bon Ramos, A.; Lee, B.W.; Cohen, S.W.; Kiani, M.K.; Iwata-Reuyl, D.; Stec, B.; Swairjo, M.A.; Biomolecules 7, E30 (2017)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
-
Bacillus subtilis
Crystallization (Commentary)
Crystallization
Organism
structure of mutant E97Q, displays an intramolecular disulfide formed between the catalytic Cys55 and a conserved Cys99 located near the active site. This structure exhibits major rearrangement of the loops responsible for substrate binding
Bacillus subtilis
Engineering
Amino acid exchange
Commentary
Organism
C99A
mutant does not compromise enzyme activity. Contrary to wild-type, peroxide-induced inactivation is irreversible
Bacillus subtilis
C99S
mutant does not compromise enzyme activity. Contrary to wild-type, peroxide-induced inactivation is irreversible
Bacillus subtilis
Inhibitors
Inhibitors
Commentary
Organism
Structure
peroxide
peroxide-induced inactivation of the wild-type enzyme is reversible with thioredoxin
Bacillus subtilis
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Bacillus subtilis
O31678
-
-
Bacillus subtilis 168
O31678
-
-
Cloned(Commentary) (protein specific)
Commentary
Organism
-
Bacillus subtilis
Crystallization (Commentary) (protein specific)
Crystallization
Organism
structure of mutant E97Q, displays an intramolecular disulfide formed between the catalytic Cys55 and a conserved Cys99 located near the active site. This structure exhibits major rearrangement of the loops responsible for substrate binding
Bacillus subtilis
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
C99A
mutant does not compromise enzyme activity. Contrary to wild-type, peroxide-induced inactivation is irreversible
Bacillus subtilis
C99S
mutant does not compromise enzyme activity. Contrary to wild-type, peroxide-induced inactivation is irreversible
Bacillus subtilis
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
peroxide
peroxide-induced inactivation of the wild-type enzyme is reversible with thioredoxin
Bacillus subtilis
Other publictions for EC 1.7.1.13
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
742061
Mohammad
Protection of the queuosine b ...
Bacillus subtilis 168, Bacillus subtilis
Biomolecules
7
E30
2017
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1
1
2
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1
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1
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742231
Gjonaj
-
Substrate and cofactor bindin ...
Escherichia coli
Catal. Sci. Technol.
6
7391-7397
2016
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1
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1
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2
1
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742900
Jung
Kinetic analysis and probing ...
Escherichia coli
J. Biol. Chem.
291
25411-25426
2016
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1
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1
3
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3
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3
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2
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743107
Li
-
Biochemical properties of a n ...
Pectobacterium carotovorum subsp. carotovorum, Pectobacterium carotovorum subsp. carotovorum PCC21
J. Mol. Catal. B
131
47-54
2016
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1
1
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1
2
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4
1
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2
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4
1
1
1
3
2
1
1
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1
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1
1
1
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1
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2
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4
1
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4
1
1
1
3
2
1
1
-
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741484
Ribeiro
-
Insight into enzymatic nitril ...
Vibrio cholerae O1, Vibrio cholerae O1 ATCC 39315
ACS Catal.
5
3740-3751
2015
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2
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4
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724767
Wilding
Targeting the substrate bindin ...
Escherichia coli
Chemistry
19
7007-7012
2013
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1
1
8
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3
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1
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2
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10
1
3
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3
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8
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3
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10
1
3
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3
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724879
Moeller
Expression and characterizatio ...
Escherichia coli
Enzyme Microb. Technol.
52
129-133
2013
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2
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2
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1
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1
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2
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1
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2
1
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2
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712770
Kim
High-resolution structure of t ...
Vibrio cholerae, Vibrio cholerae ATCC 39315
J. Mol. Biol.
404
127-137
2010
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1
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660634
Swairjo
Crystallization and preliminar ...
Bacillus subtilis
Acta Crystallogr. Sect. F
F61
945-948
2005
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1
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663244
van Lanen
From cyclohydrolase to oxidore ...
Bacillus subtilis, Escherichia coli
Proc. Natl. Acad. Sci. USA
102
4264-4269
2005
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2
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1
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2
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7
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2
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2
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1
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662983
Okada
Structure determination of a n ...
Escherichia coli
Nucleic Acids Res.
5
2289-2296
1978
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1
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1
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662984
Noguchi
Isolation of Q nucleoside prec ...
Escherichia coli
Nucleic Acids Res.
5
4215-4223
1978
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1
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662966
Kuchino
Biosynthesis of the modified n ...
Salmonella enterica subsp. enterica serovar Typhimurium
Nucleic Acids Res.
3
393-398
1976
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