BRENDA - Enzyme Database
show all sequences of 1.8.4.8

Crystal structure of phosphoadenylyl sulphate (PAPS) reductase: a new family of adenine nucleotide alpha hydrolases

Savage, H.; Montoya, G.; Svensson, C.; Schwenn, J.D.; Sinning, I.; Structure 5, 895-906 (1997)

Data extracted from this reference:

Crystallization (Commentary)
Crystallization (Commentary)
Organism
crystal structure at 2.0 A. The enzyme shows striking similarity to the structure of the ATP pyrophosphatase domain of GMP synthetase, indicating that both enzyme families have evolved from a common ancestral nucleotide-binding fold
Escherichia coli
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin
Escherichia coli
essential step in the biosynthesis of Cys in E. coli. Blocking of the enzyme inhibits cell growth
?
-
-
-
Organism
Organism
UniProt
Commentary
Textmining
Escherichia coli
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin
-
133776
Escherichia coli
adenosine-3',5'-bisphosphate + oxidized thioredoxin + sulfite
-
-
-
-
5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin
essential step in the biosynthesis of Cys in E. coli. Blocking of the enzyme inhibits cell growth
133776
Escherichia coli
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
dimer
homodimer, each monomer consisting of a six-stranded beta-sheet surrounded by alpha-helices, crystallographic date
Escherichia coli
Crystallization (Commentary) (protein specific)
Crystallization
Organism
crystal structure at 2.0 A. The enzyme shows striking similarity to the structure of the ATP pyrophosphatase domain of GMP synthetase, indicating that both enzyme families have evolved from a common ancestral nucleotide-binding fold
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin
Escherichia coli
essential step in the biosynthesis of Cys in E. coli. Blocking of the enzyme inhibits cell growth
?
-
-
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin
-
133776
Escherichia coli
adenosine-3',5'-bisphosphate + oxidized thioredoxin + sulfite
-
-
-
-
5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin
essential step in the biosynthesis of Cys in E. coli. Blocking of the enzyme inhibits cell growth
133776
Escherichia coli
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
homodimer, each monomer consisting of a six-stranded beta-sheet surrounded by alpha-helices, crystallographic date
Escherichia coli
Other publictions for EC 1.8.4.8
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
Synonyms
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)
742273
Berndt
-
The specificity of thioredoxi ...
Escherichia coli
Chem. Sci.
6
7049-7058
2015
-
-
-
-
-
-
-
9
-
-
-
-
-
1
-
-
-
-
-
-
-
-
10
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
9
-
-
-
-
-
-
-
-
-
-
-
-
10
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
712502
Bhave
Spectroscopic studies on the [ ...
Mycobacterium tuberculosis
J. Biol. Chem.
286
1216-1226
2011
-
1
1
-
1
-
-
-
-
1
-
-
-
3
-
-
1
-
-
-
-
-
1
-
3
-
-
-
-
-
-
-
1
-
-
-
-
1
1
1
-
1
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
2
2
698950
Chung
Interaction domain on thioredo ...
Pseudomonas aeruginosa
J. Biol. Chem.
284
31181-31189
2009
-
-
1
-
-
-
-
1
-
-
-
-
-
4
-
-
1
-
-
-
-
-
2
-
3
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
685145
Chartron
3-Phosphoadenosine-5-phosphosu ...
Escherichia coli
Biochemistry
46
3942-3951
2007
-
-
1
1
-
-
-
-
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
670348
Mansouri-Bauly
Sulfur uptake in the ectomycor ...
Laccaria bicolor, Laccaria bicolor S238N
Mycorrhiza
16
421-427
2006
1
-
-
-
-
-
1
-
-
-
-
-
-
9
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
659441
Berndt
Characterization and reconstit ...
Bacillus subtilis
J. Biol. Chem.
279
7850-7855
2004
-
-
1
-
-
1
-
8
-
1
1
3
-
2
1
-
-
-
-
-
1
-
3
1
3
-
-
-
8
1
-
-
2
-
-
-
-
-
1
2
-
-
1
-
-
-
8
-
1
1
3
-
1
-
-
-
-
1
-
3
1
-
-
-
8
1
-
-
-
-
-
-
-
-
-
659214
Lillig
Redox regulation of 3'-phospho ...
Escherichia coli
J. Biol. Chem.
278
22325-22330
2003
1
-
1
-
1
-
1
-
-
-
-
3
-
2
-
-
1
1
-
-
-
-
3
-
2
1
-
-
-
1
-
-
2
-
-
-
1
-
1
2
-
1
-
-
1
-
-
-
-
-
3
-
-
-
1
-
-
-
-
3
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
393953
Kopriva
The presence of an iron-sulfur ...
Escherichia coli
J. Biol. Chem.
277
21786-21791
2002
-
-
1
-
-
-
-
-
-
1
-
2
-
12
-
-
1
-
-
-
-
-
3
-
2
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
1
-
2
-
-
-
1
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
659140
Lillig
New thioredoxins and glutaredo ...
Escherichia coli
J. Biol. Chem.
274
7695-7698
1999
-
-
1
-
-
-
-
6
-
-
-
2
-
4
-
-
1
1
-
-
1
-
5
1
2
1
-
-
1
1
-
-
2
-
-
-
-
-
1
2
-
-
-
-
-
-
6
-
-
-
2
-
-
-
1
-
-
1
-
5
1
1
-
-
1
1
-
-
-
-
-
-
-
-
-
133777
Montoya
Crystallization and preliminar ...
Escherichia coli
Acta Crystallogr. Sect. D
54
281-283
1998
-
-
-
1
-
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
133776
Savage
Crystal structure of phosphoad ...
Escherichia coli
Structure
5
895-906
1997
-
-
-
1
-
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
133778
Berendt
Reaction mechanism of thioredo ...
Escherichia coli
Eur. J. Biochem.
233
347-356
1995
-
-
-
-
3
-
4
2
-
-
-
-
-
2
-
-
-
1
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
4
-
2
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
133779
Niehaus
Primary structure of Synechoco ...
Synechococcus sp., Synechococcus sp. PCC 7942
Plant Mol. Biol.
20
1179-1183
1992
-
-
-
-
-
-
-
-
-
-
1
-
-
25
-
-
-
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
133780
Krone
Characterisation of the gene c ...
Escherichia coli
Mol. Gen. Genet.
225
314-319
1991
-
-
1
-
-
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
133775
Schwenn
Yeast PAPS reductase: properti ...
Saccharomyces cerevisiae
Arch. Microbiol.
150
313-319
1988
-
-
-
-
-
-
-
4
-
-
-
-
-
3
-
-
1
1
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
1
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-