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show all sequences of 5.4.99.24

Crystallisation and characterization of a fragment of pseudouridine synthase RluC from Escherichia coli

Corollo, D.; Blair-Johnson, M.; Conrad, J.; Friedler, T.; Sun, D.; Wang, L.; Ofengand, J.; Fenna, R.; Acta Crystallogr. Sect. D 55, 302-304 (1999)
No PubMed abstract available

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
-
Escherichia coli
Crystallization (Commentary)
Crystallization
Organism
a proteolytically derived fragment of the enzyme consisting of residues 89-319 retains catalytic activity. Crystals of this fragment, grown by precipitation with sodium acetate at pH 8.0, belong to space group P321, with unit-cell dimensions a = b = 97.1, c = 86.3 A and have two molecules in the crystallographic asymmetric unit. Crystals diffract X-rays to at least 2.3 A resolution and appear suitable for crystal structure determination
Escherichia coli
Engineering
Amino acid exchange
Commentary
Organism
additional information
a proteolytically derived fragment of the enzyme consisting of residues 89-319 retains catalytic activity
Escherichia coli
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
P0AA39
-
-
Purification (Commentary)
Commentary
Organism
-
Escherichia coli
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
23S rRNA uridine955/uridine2504/uridine2580
-
5857
Escherichia coli
23S rRNA pseudouridine955/pseudouridine2504/pseudouridine2580
-
-
-
?
Cloned(Commentary) (protein specific)
Commentary
Organism
-
Escherichia coli
Crystallization (Commentary) (protein specific)
Crystallization
Organism
a proteolytically derived fragment of the enzyme consisting of residues 89-319 retains catalytic activity. Crystals of this fragment, grown by precipitation with sodium acetate at pH 8.0, belong to space group P321, with unit-cell dimensions a = b = 97.1, c = 86.3 A and have two molecules in the crystallographic asymmetric unit. Crystals diffract X-rays to at least 2.3 A resolution and appear suitable for crystal structure determination
Escherichia coli
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
a proteolytically derived fragment of the enzyme consisting of residues 89-319 retains catalytic activity
Escherichia coli
Purification (Commentary) (protein specific)
Commentary
Organism
-
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
23S rRNA uridine955/uridine2504/uridine2580
-
5857
Escherichia coli
23S rRNA pseudouridine955/pseudouridine2504/pseudouridine2580
-
-
-
?
Other publictions for EC 5.4.99.24
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)
748788
Leppik
Random pseuoduridylation in v ...
Escherichia coli
Nucleic Acids Res.
45
6098-6108
2017
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1
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2
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1
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1
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699543
Toh
An indigenous posttranscriptio ...
Escherichia coli
J. Mol. Biol.
380
593-597
2008
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1
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1
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1
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704271
Jiang
Identification of novel Escher ...
Escherichia coli
J. Bacteriol.
189
3434-3444
2007
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1
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1
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1
1
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702207
Mizutani
Crystal structures of the cata ...
Escherichia coli
Biochemistry
43
4454-4463
2004
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1
1
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1
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3
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1
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5857
Corollo
-
Crystallisation and characteri ...
Escherichia coli
Acta Crystallogr. Sect. D
55
302-304
1999
-
-
1
1
1
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1
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1
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1
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1
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1
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702195
Huang
Identification of two Escheric ...
Escherichia coli
Biochemistry
37
15951-15957
1998
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1
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1
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1
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1
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704389
Conrad
The rluC gene of Escherichia c ...
Escherichia coli
J. Biol. Chem.
273
18562-18566
1998
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1
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