BRENDA - Enzyme Database show
show all sequences of 2.1.1.177

A comparison of the folding of two knotted proteins: YbeA and YibK

Mallam, A.L.; Jackson, S.E.; J. Mol. Biol. 366, 650-665 (2007)

Data extracted from this reference:

Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
36800
-
gel filtration
Escherichia coli
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
P0A8I8
-
-
Subunits
Subunits
Commentary
Organism
homodimer
belongs to the alpha/beta-knot superfamily of proteins that are dimeric in solution. The enzyme folds via an intermediate state populated under equilibrium conditions that is monomeric and considerably structured. The unfolding/refolding kinetics of YbeA involves two phases attributed to the formation of a monomeric intermediate state and a dimerisation step
Escherichia coli
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
36800
-
gel filtration
Escherichia coli
Subunits (protein specific)
Subunits
Commentary
Organism
homodimer
belongs to the alpha/beta-knot superfamily of proteins that are dimeric in solution. The enzyme folds via an intermediate state populated under equilibrium conditions that is monomeric and considerably structured. The unfolding/refolding kinetics of YbeA involves two phases attributed to the formation of a monomeric intermediate state and a dimerisation step
Escherichia coli
Other publictions for EC 2.1.1.177
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)
706718
Ero
Identification of pseudouridin ...
Escherichia coli
RNA
14
2223-2233
2008
-
-
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-
-
-
-
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1
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4
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1
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-
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2
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1
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1
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1
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1
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2
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1
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1
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1
1
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706719
Purta
YbeA is the m3Psi methyltransf ...
Escherichia coli
RNA
14
2234-2244
2008
-
-
1
-
-
-
-
-
-
-
-
1
-
5
-
-
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1
-
-
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1
1
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1
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1
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1
1
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2
2
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705114
Mallam
A comparison of the folding of ...
Escherichia coli
J. Mol. Biol.
366
650-665
2007
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