BRENDA - Enzyme Database
show all sequences of 2.5.1.65

Crystallization and preliminary X-ray diffraction analysis of O-acetylserine sulfhydrylase from Aeropyrum pernix K1

Mino, K.; Oda, Y.; Ataka, M.; Ishikawa, K.; Acta Crystallogr. Sect. D 59, 338-340 (2003)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
overexpression in Escherichia coli; overexpression in Escherichia coli Rosetta (DE3)
Aeropyrum pernix
Crystallization (Commentary)
Crystallization
Organism
hanging-drop vapor-diffusion method; purified recombinant enzyme, optimization of crystallization method, hanging drop vapour diffusion method, enzyme in 50 mM potassium phosphate buffer pH 7.5, containing 0.2 mM pyridoxal 5'-phosphate and 0.05% sodium azide, 0.0015 ml of enzyme and reservoir solution, containing 0.1 M sodium cacodylate pH 7.4, 0.1 M sodium acetate and 30% v/v PEG 8000, are equilibrated against 0.5 ml of reservoir solution at 295°C, 2 weeks, cryoprotection by 10% v/v glycerol, X-ray diffraction structure determination and analysis at 2.2 A resolution
Aeropyrum pernix
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Aeropyrum pernix
L-cysteine biosynthesis
?
-
-
-
O-acetyl-L-serine + hydrogen sulfide
Aeropyrum pernix
-
L-cysteine + acetate
-
-
?
O-phospho-L-serine + hydrogen sulfide
Aeropyrum pernix
-
L-cysteine + phosphate
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Aeropyrum pernix
-
-
-
Purification (Commentary)
Commentary
Organism
recombinant enzyme from Escherichia coli; recombinant OASS
Aeropyrum pernix
Reaction
Reaction
Commentary
Organism
O-phospho-L-serine + hydrogen sulfide = L-cysteine + phosphate
a pyridoxal-phosphate protein, the enzyme from Aeropyrum pernix acts on both O-phospho-L-serine and O3-acetyl-L-serine, in contrast with EC 2.5.1.47, cysteine synthase, which acts only on O3-acetyl-L-serine
Aeropyrum pernix
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
L-cysteine biosynthesis
654085
Aeropyrum pernix
?
-
-
-
-
O-acetyl-L-serine + hydrogen sulfide
-
654085
Aeropyrum pernix
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + sulfide
-
654085
Aeropyrum pernix
L-cysteine + acetic acid
-
-
-
?
O-phospho-L-serine + hydrogen sulfide
-
654085
Aeropyrum pernix
L-cysteine + phosphate
-
-
-
?
Subunits
Subunits
Commentary
Organism
dimer
-
Aeropyrum pernix
Cofactor
Cofactor
Commentary
Organism
Structure
pyridoxal 5'-phosphate
required
Aeropyrum pernix
Cloned(Commentary) (protein specific)
Commentary
Organism
overexpression in Escherichia coli; overexpression in Escherichia coli Rosetta (DE3)
Aeropyrum pernix
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
pyridoxal 5'-phosphate
required
Aeropyrum pernix
Crystallization (Commentary) (protein specific)
Crystallization
Organism
hanging-drop vapor-diffusion method; purified recombinant enzyme, optimization of crystallization method, hanging drop vapour diffusion method, enzyme in 50 mM potassium phosphate buffer pH 7.5, containing 0.2 mM pyridoxal 5'-phosphate and 0.05% sodium azide, 0.0015 ml of enzyme and reservoir solution, containing 0.1 M sodium cacodylate pH 7.4, 0.1 M sodium acetate and 30% v/v PEG 8000, are equilibrated against 0.5 ml of reservoir solution at 295°C, 2 weeks, cryoprotection by 10% v/v glycerol, X-ray diffraction structure determination and analysis at 2.2 A resolution
Aeropyrum pernix
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Aeropyrum pernix
L-cysteine biosynthesis
?
-
-
-
O-acetyl-L-serine + hydrogen sulfide
Aeropyrum pernix
-
L-cysteine + acetate
-
-
?
O-phospho-L-serine + hydrogen sulfide
Aeropyrum pernix
-
L-cysteine + phosphate
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant enzyme from Escherichia coli; recombinant OASS
Aeropyrum pernix
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
L-cysteine biosynthesis
654085
Aeropyrum pernix
?
-
-
-
-
O-acetyl-L-serine + hydrogen sulfide
-
654085
Aeropyrum pernix
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + sulfide
-
654085
Aeropyrum pernix
L-cysteine + acetic acid
-
-
-
?
O-phospho-L-serine + hydrogen sulfide
-
654085
Aeropyrum pernix
L-cysteine + phosphate
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
-
Aeropyrum pernix
Other publictions for EC 2.5.1.65
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)
738193
Takeda
Role of F225 in O-phosphoserin ...
Aeropyrum pernix, Aeropyrum pernix DSM 11879
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20
733-745
2016
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-
-
1
1
-
-
4
-
-
-
2
-
5
-
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1
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-
-
10
-
1
-
-
7
1
-
-
1
-
-
-
-
-
-
1
1
1
-
-
-
-
4
-
-
-
2
-
-
-
-
-
-
-
-
10
-
1
-
-
7
1
-
-
-
-
1
1
-
7
7
737868
Nakamura
Thermostability and reactivity ...
Aeropyrum pernix, Aeropyrum pernix DSM 11879
Biosci. Biotechnol. Biochem.
79
1280-1286
2015
-
-
1
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-
-
-
-
-
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-
2
2
6
-
-
1
1
-
-
-
-
6
-
1
-
1
-
1
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
2
2
-
-
1
-
-
-
-
6
-
1
-
1
-
1
-
-
-
-
1
1
-
-
-
738534
Steiner
CysK2 from Mycobacterium tuber ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
J. Bacteriol.
196
3410-3420
2014
-
-
1
-
2
-
-
8
-
-
-
2
-
3
-
-
1
1
-
-
-
-
6
1
1
-
-
4
2
-
-
1
-
-
-
-
-
1
1
-
2
-
-
-
-
8
-
-
-
2
-
-
-
1
-
-
-
-
6
1
1
-
-
4
2
-
-
-
-
2
2
-
5
5
722990
Nakamura
Structural analysis of the sub ...
Aeropyrum pernix
J. Mol. Biol.
422
33-44
2012
-
-
1
1
11
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
1
11
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
685195
OLeary
O-Phospho-l-serine and the thi ...
Mycobacterium tuberculosis
Biochemistry
47
11606-11615
2008
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
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3
-
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-
2
-
-
-
-
-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
687773
Agren
Cysteine synthase (CYSM) of My ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
J. Biol. Chem.
283
31567-31574
2008
-
-
1
1
1
-
-
-
-
-
-
4
-
6
-
-
1
-
-
-
-
-
8
-
-
-
-
1
-
-
-
1
-
-
-
-
-
2
2
2
2
-
-
-
-
-
-
-
-
4
-
-
-
1
-
-
-
-
8
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
702213
Jurgenson
Crystal structure of a sulfur ...
Mycobacterium tuberculosis
Biochemistry
47
10354-10364
2008
-
-
1
1
1
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
1
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-
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-
-
-
-
1
-
-
-
-
-
1
1
1
1
-
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-
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-
-
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-
-
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-
1
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-
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-
1
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-
-
-
-
-
-
-
-
-
-
659728
Oda
Three-dimensional structure of ...
Aeropyrum pernix
J. Mol. Biol.
351
334-344
2005
-
-
1
1
1
-
-
-
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-
1
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7
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1
1
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-
4
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4
1
1
-
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-
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-
1
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-
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1
1
1
1
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1
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1
-
-
4
-
4
1
1
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-
-
-
-
-
-
-
-
-
-
-
-
637385
Mino
Characterization of a novel th ...
Aeropyrum pernix
J. Bacteriol.
185
2277-2284
2003
-
-
1
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-
-
-
3
-
-
2
1
-
1
-
-
1
-
-
-
1
1
4
1
-
-
1
2
1
-
4
1
-
-
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-
1
1
-
-
-
-
-
-
3
-
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2
1
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-
1
-
-
1
1
4
1
-
-
1
2
1
-
4
-
-
-
-
-
-
-
654085
Mino
Crystallization and preliminar ...
Aeropyrum pernix
Acta Crystallogr. Sect. D
59
338-340
2003
-
-
1
1
-
-
-
-
-
-
-
3
-
1
-
-
1
1
-
-
-
-
4
1
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
1
-
-
-
-
-
-
-
-
-
3
-
-
-
1
-
-
-
-
4
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
655576
Mino
A novel O-phospho-L-serine sul ...
Aeropyrum pernix
FEBS Lett.
551
133-138
2003
1
-
1
-
-
-
23
10
-
-
1
3
-
1
-
-
1
1
-
-
1
-
13
1
3
-
1
3
1
-
-
1
-
-
-
1
-
1
1
-
-
-
-
23
-
10
-
-
1
3
-
-
-
1
-
-
1
-
13
1
3
-
1
3
1
-
-
-
-
-
-
-
-
-