BRENDA - Enzyme Database
show all sequences of 2.5.1.65

Thermostability and reactivity in organic solvent of O-phospho-L-serine sulfhydrylase from hyperthermophilic archaeon Aeropyrum pernix K1

Nakamura, T.; Asai, S.; Nakata, K.; Kunimoto, K.; Oguri, M.; Ishikawa, K.; Biosci. Biotechnol. Biochem. 79, 1280-1286 (2015)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21 (DE3) pLysS
Aeropyrum pernix
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
O-phospho-L-serine + hydrogen sulfide
Aeropyrum pernix
-
L-cysteine + phosphate
-
-
?
O-phospho-L-serine + hydrogen sulfide
Aeropyrum pernix DSM 11879
-
L-cysteine + phosphate
-
-
?
Organic Solvent Stability
Organic Solvent
Commentary
Organism
1,4-dioxane
the activity of enzyme OPSS increases in the reaction mixture containing the organic solvent, such as N,N-dimethylformamide and 1,4-dioxane
Aeropyrum pernix
N,N-dimethylformamide
the activity of enzyme OPSS increases in the reaction mixture containing the organic solvent, such as N,N-dimethylformamide and 1,4-dioxane
Aeropyrum pernix
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Aeropyrum pernix
Q9YBL2
-
-
Aeropyrum pernix DSM 11879
Q9YBL2
-
-
Purification (Commentary)
Commentary
Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21 (DE3) pLysS by nickel affinity chromatography
Aeropyrum pernix
Reaction
Reaction
Commentary
Organism
O-phospho-L-serine + hydrogen sulfide = L-cysteine + phosphate
ping-pong bi-bi mechanism
Aeropyrum pernix
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
OPSS is able to catalyze the synthetic reactions of various unnatural amino acids from OPS and nucleophiles that can substitute for sulfide
737868
Aeropyrum pernix
?
-
-
-
-
additional information
OPSS is able to catalyze the synthetic reactions of various unnatural amino acids from OPS and nucleophiles that can substitute for sulfide
737868
Aeropyrum pernix DSM 11879
?
-
-
-
-
O-phospho-L-serine + hydrogen sulfide
-
737868
Aeropyrum pernix
L-cysteine + phosphate
-
-
-
?
O-phospho-L-serine + hydrogen sulfide
residue Arg297 near the entrance of the active site and is important for O-phospho-L-serine substrate recognition
737868
Aeropyrum pernix
L-cysteine + phosphate
-
-
-
?
O-phospho-L-serine + hydrogen sulfide
-
737868
Aeropyrum pernix DSM 11879
L-cysteine + phosphate
-
-
-
?
O-phospho-L-serine + hydrogen sulfide
residue Arg297 near the entrance of the active site and is important for O-phospho-L-serine substrate recognition
737868
Aeropyrum pernix DSM 11879
L-cysteine + phosphate
-
-
-
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
80
-
assay at
Aeropyrum pernix
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
-
100
purified recombinant His-tagged enzyme, 1 h, completely stable at
Aeropyrum pernix
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.7
-
assay at
Aeropyrum pernix
Cofactor
Cofactor
Commentary
Organism
Structure
pyridoxal 5'-phosphate
linked to lysine K127 as an internal Schiff base at the active site
Aeropyrum pernix
Cloned(Commentary) (protein specific)
Commentary
Organism
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21 (DE3) pLysS
Aeropyrum pernix
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
pyridoxal 5'-phosphate
linked to lysine K127 as an internal Schiff base at the active site
Aeropyrum pernix
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
O-phospho-L-serine + hydrogen sulfide
Aeropyrum pernix
-
L-cysteine + phosphate
-
-
?
O-phospho-L-serine + hydrogen sulfide
Aeropyrum pernix DSM 11879
-
L-cysteine + phosphate
-
-
?
Organic Solvent Stability (protein specific)
Organic Solvent
Commentary
Organism
1,4-dioxane
the activity of enzyme OPSS increases in the reaction mixture containing the organic solvent, such as N,N-dimethylformamide and 1,4-dioxane
Aeropyrum pernix
N,N-dimethylformamide
the activity of enzyme OPSS increases in the reaction mixture containing the organic solvent, such as N,N-dimethylformamide and 1,4-dioxane
Aeropyrum pernix
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21 (DE3) pLysS by nickel affinity chromatography
Aeropyrum pernix
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
OPSS is able to catalyze the synthetic reactions of various unnatural amino acids from OPS and nucleophiles that can substitute for sulfide
737868
Aeropyrum pernix
?
-
-
-
-
additional information
OPSS is able to catalyze the synthetic reactions of various unnatural amino acids from OPS and nucleophiles that can substitute for sulfide
737868
Aeropyrum pernix DSM 11879
?
-
-
-
-
O-phospho-L-serine + hydrogen sulfide
-
737868
Aeropyrum pernix
L-cysteine + phosphate
-
-
-
?
O-phospho-L-serine + hydrogen sulfide
residue Arg297 near the entrance of the active site and is important for O-phospho-L-serine substrate recognition
737868
Aeropyrum pernix
L-cysteine + phosphate
-
-
-
?
O-phospho-L-serine + hydrogen sulfide
-
737868
Aeropyrum pernix DSM 11879
L-cysteine + phosphate
-
-
-
?
O-phospho-L-serine + hydrogen sulfide
residue Arg297 near the entrance of the active site and is important for O-phospho-L-serine substrate recognition
737868
Aeropyrum pernix DSM 11879
L-cysteine + phosphate
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
80
-
assay at
Aeropyrum pernix
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
-
100
purified recombinant His-tagged enzyme, 1 h, completely stable at
Aeropyrum pernix
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.7
-
assay at
Aeropyrum pernix
General Information
General Information
Commentary
Organism
additional information
Intramolecular electrostatic interaction of enzyme OPSS, overview
Aeropyrum pernix
General Information (protein specific)
General Information
Commentary
Organism
additional information
Intramolecular electrostatic interaction of enzyme OPSS, overview
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
Extremophiles
20
733-745
2016
-
-
-
1
1
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-
4
-
-
-
2
-
5
-
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-
1
-
-
-
-
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
-
-
-
-
-
-
-
-
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
-
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-
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
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-
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-
1
1
1
1
-
-
-
-
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-
1
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-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
659728
Oda
Three-dimensional structure of ...
Aeropyrum pernix
J. Mol. Biol.
351
334-344
2005
-
-
1
1
1
-
-
-
-
-
-
1
-
7
-
-
1
1
-
-
4
-
4
1
1
-
-
-
-
-
-
1
-
-
-
-
-
1
1
1
1
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
4
-
4
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
637385
Mino
Characterization of a novel th ...
Aeropyrum pernix
J. Bacteriol.
185
2277-2284
2003
-
-
1
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-
-
-
3
-
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2
1
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1
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1
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1
1
4
1
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1
2
1
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4
1
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-
1
1
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-
-
-
-
3
-
-
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
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1
1
-
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4
1
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1
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1
1
1
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3
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1
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4
1
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-
-
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-
-
-
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-
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
-
-
-
-
-
-
-
-
-