BRENDA - Enzyme Database
show all sequences of 2.5.1.65

A novel O-phospho-L-serine sulfhydrylation reaction catalyzed by O-acetylserine sulfhydrylase from Aeropyrum pernix K1

Mino, K.; Ishikawa, K.; FEBS Lett. 551, 133-138 (2003)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
dithiothreitol
slightly activates the O-phospho-L-serine sulfhydrylation reaction
Aeropyrum pernix
Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli Rosetta (DE3)
Aeropyrum pernix
Inhibitors
Inhibitors
Commentary
Organism
Structure
3-chloro-D-alanine
18% inhibition of the O-acetyl-L-serine sulfhydrylation reaction
Aeropyrum pernix
3-Cyano-L-alanine
42% inhibition of the O-acetyl-L-serine sulfhydrylation reaction
Aeropyrum pernix
Cd2+
slightly inhibites both O-acetyl-L-serine sulfhydrylation and O-phospho-L-serine sulfhydrylation
Aeropyrum pernix
CdCl2
25°C, 10 min, 26% inhibition of the O-phospho-L-serine sulfhydrylation reaction, 15% inhibition of the O-acetyl-L-serine sulfhydrylation reaction
Aeropyrum pernix
Co2+
strongly inhibits O-acetyl-L-serine sulfhydrylation, moderately inhibites O-phospho-L-serine sulfhydrylation
Aeropyrum pernix
CoCl2
25°C, 10 min, 61% inhibition of the O-phospho-L-serine sulfhydrylation reaction, 98.8% inhibition of the O-acetyl-L-serine sulfhydrylation reaction
Aeropyrum pernix
Cu2+
strongly inhibits O-acetyl-L-serine sulfhydrylation, moderately inhibites O-phospho-L-serine sulfhydrylation
Aeropyrum pernix
CuCl2
25°C, 10 min, 79% inhibition of the O-phospho-L-serine sulfhydrylation reaction, 98.7% inhibition of the O-acetyl-L-serine sulfhydrylation reaction
Aeropyrum pernix
Fe2+
slightly inhibites both O-acetyl-L-serine sulfhydrylation and O-phospho-L-serine sulfhydrylation
Aeropyrum pernix
Fe3+
strongly inhibits O-acetyl-L-serine sulfhydrylation, slightly inhibites O-phospho-L-serine sulfhydrylation
Aeropyrum pernix
FeCl2
25°C, 10 min, 20% inhibition of the O-phospho-L-serine sulfhydrylation reaction, 27% inhibition of the O-acetyl-L-serine sulfhydrylation reaction
Aeropyrum pernix
FeCl3
25°C, 10 min, 25% inhibition of the O-phospho-L-serine sulfhydrylation reaction, 96.1% inhibition of the O-acetyl-L-serine sulfhydrylation reaction
Aeropyrum pernix
Hg2+
strongly inhibites both O-acetyl-L-serine sulfhydrylation and O-phospho-L-serine sulfhydrylation
Aeropyrum pernix
HgCl2
25°C, 10 min, 98.3% inhibition of the O-phospho-L-serine sulfhydrylation reaction, 80% inhibition of the O-acetyl-L-serine sulfhydrylation reaction
Aeropyrum pernix
additional information
no inhibition by O-phospho-D-serine, EDTA, 2-mercaptoethanol, DTT, NEM, PCMB, and Gd3+, while Ca2+, K+, Na+, Mn2+, and Mg2+ are poor inhibitors; no inhibition of the O-acetyl-L-serine sulfhydrylation reaction by O-phospho-D-serine
Aeropyrum pernix
Ni2+
strongly inhibits O-acetyl-L-serine sulfhydrylation, slightly inhibites O-phospho-L-serine sulfhydrylation
Aeropyrum pernix
NiCl2
25°C, 10 min, 15% inhibition of the O-phospho-L-serine sulfhydrylation reaction, almost complete inhibition of the O-acetyl-L-serine sulfhydrylation reaction
Aeropyrum pernix
O-benzyl-L-serine
36% inhibition of the O-acetyl-L-serine sulfhydrylation reaction
Aeropyrum pernix
O-tert-butyl-L-serine
49% inhibition of the O-acetyl-L-serine sulfhydrylation reaction
Aeropyrum pernix
Pb(CH3COO)2
25°C, 10 min, 95% inhibition of the O-phospho-L-serine sulfhydrylation reaction, 88% inhibition of the O-acetyl-L-serine sulfhydrylation reaction
Aeropyrum pernix
Pb2+
strongly inhibites both O-acetyl-L-serine sulfhydrylation and O-phospho-L-serine sulfhydrylation
Aeropyrum pernix
Zn2+
slightly inhibites both O-acetyl-L-serine sulfhydrylation and O-phospho-L-serine sulfhydrylation
Aeropyrum pernix
ZnCl2
25°C, 10 min, 23% inhibition of the O-phospho-L-serine sulfhydrylation reaction, 25% inhibition of the O-acetyl-L-serine sulfhydrylation reaction
Aeropyrum pernix
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetics; ping-pong bi-bi mechanism
Aeropyrum pernix
0.25
-
hydrogen sulfide
pH 7.6, 60°C, with O-acetyl-L-serine
Aeropyrum pernix
0.25
-
Sulfide
60°C, O-acetyl-L-serine sulfhydrylation reaction
Aeropyrum pernix
5
-
hydrogen sulfide
pH 7.6, 60°C, with O-phospho-L-serine
Aeropyrum pernix
5
-
Sulfide
60°C, O-phospho-L-serine sulfhydrylation reaction
Aeropyrum pernix
12.5
-
hydrogen sulfide
pH 7.6, 85°C, with O-phospho-L-serine
Aeropyrum pernix
12.5
-
Sulfide
85°C, O-phospho-L-serine sulfhydrylation reaction
Aeropyrum pernix
21
-
O-acetyl-L-serine
60°C; pH 7.6, 60°C
Aeropyrum pernix
200
-
O-phospho-L-serine
60°C; pH 7.6, 60°C
Aeropyrum pernix
250
-
O-phospho-L-serine
85°C; pH 7.6, 85°C
Aeropyrum pernix
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
42000
-
2 * 42000
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
enzyme is involved in L-cysteine biosynthesis, pathway overview
L-cysteine + acetate
-
-
ir
O-phospho-L-serine + hydrogen sulfide
Aeropyrum pernix
enzyme is involved in L-cysteine biosynthesis, pathway overview
L-cysteine + phosphate
-
-
ir
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Aeropyrum pernix
-
; hyperthermophilic archeon
-
Purification (Commentary)
Commentary
Organism
recombinant OASS
Aeropyrum pernix
Reaction
Reaction
Commentary
Organism
O-phospho-L-serine + hydrogen sulfide = L-cysteine + phosphate
ping-pong bi-bi mechanism
Aeropyrum pernix
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
54.5
-
60°C, O-acetyl-L-serine sulfhydrylation reaction, recombinant OASS
Aeropyrum pernix
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3-chloro-L-alanine + hydrogen sulfide
-
655576
Aeropyrum pernix
?
-
-
-
ir
3-chloro-L-alanine + sulfide
heat-labile substrate, 173% of activity compared with O-acetyl-L-serine as substrate
655576
Aeropyrum pernix
?
-
-
-
?
L-azaserine + hydrogen sulfide
O-phospho-L-serine is a heat-stable substrate
655576
Aeropyrum pernix
?
-
-
-
ir
L-azaserine + sulfide
same activity as with O-acetyl-L-serine as substrate
655576
Aeropyrum pernix
?
-
-
-
?
additional information
L-cysteine biosynthesis
655576
Aeropyrum pernix
?
-
-
-
-
additional information
not: 3-chloro-D-alanine, 3-cyano-L-alanine, O-benzyl-L-serine, O-tert-butyl-L-serine, O-phospho-D-serine, O-succinyl-L-homoserine, L-homoserine
655576
Aeropyrum pernix
?
-
-
-
-
additional information
substrate specificity, no activity with 3-chloro-D-alanine, 3-cyano-L-alanine, O-benzyl-L-serine, O-tert-butyl-L-serine, O-phospho-D-serine, O-succinyl-L-homoserine, and L-homoserine
655576
Aeropyrum pernix
?
-
-
-
-
O-acetyl-L-serine + hydrogen sulfide
enzyme is involved in L-cysteine biosynthesis, pathway overview
655576
Aeropyrum pernix
L-cysteine + acetate
-
-
-
ir
O-acetyl-L-serine + hydrogen sulfide
O-acetyl-L-serine is a heat-labile substrate
655576
Aeropyrum pernix
L-cysteine + acetate
-
-
-
ir
O-acetyl-L-serine + sulfide
heat-labile substrate
655576
Aeropyrum pernix
L-cysteine + acetic acid
-
-
-
?
O-phospho-L-serine + hydrogen sulfide
enzyme is involved in L-cysteine biosynthesis, pathway overview
655576
Aeropyrum pernix
L-cysteine + phosphate
-
-
-
ir
O-phospho-L-serine + hydrogen sulfide
O-phospho-L-serine is a heat-stable substrate
655576
Aeropyrum pernix
L-cysteine + phosphate
-
-
-
ir
O-phospho-L-serine + sulfide
heat-stabile substrate, 219% of activity compared with O-acetyl-L-serine as substrate, best substrate at pH 6.7 and 60°C, formation of an alpha-aminoacrylate intermediate between O-phospho-L-serine and pyridoxal 5’-phosphate
655576
Aeropyrum pernix
L-cysteine + phosphate
-
-
-
?
Subunits
Subunits
Commentary
Organism
dimer
2 * 42000
Aeropyrum pernix
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
70
-
sulfhydrylation of 3-chloro-L-alanine; with substrate 3-chloro-L-alanine
Aeropyrum pernix
80
-
sulfhydrylation of L-azaserine; with substrate L-azaserine
Aeropyrum pernix
90
-
sulfhydrylation of O-phospho-L-serine; with substrate O-phospho-L-serine
Aeropyrum pernix
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
90
-
50% of maximum activity with 3-chloro-L-alanine as substrate
Aeropyrum pernix
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
156
-
O-acetyl-L-serine
60°C; pH 7.6, 60°C
Aeropyrum pernix
3050
-
O-phospho-L-serine
60°C; pH 7.6, 60°C
Aeropyrum pernix
14000
-
O-phospho-L-serine
85°C; pH 7.6, 85°C
Aeropyrum pernix
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.3
8.1
at 85°C; dependent on the substrate, overview
Aeropyrum pernix
Cofactor
Cofactor
Commentary
Organism
Structure
pyridoxal 5'-phosphate
dependent on; pyridoxal 5'-phosphate-dependent
Aeropyrum pernix
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
dithiothreitol
slightly activates the O-phospho-L-serine sulfhydrylation reaction
Aeropyrum pernix
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli Rosetta (DE3)
Aeropyrum pernix
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
pyridoxal 5'-phosphate
dependent on; pyridoxal 5'-phosphate-dependent
Aeropyrum pernix
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
3-chloro-D-alanine
18% inhibition of the O-acetyl-L-serine sulfhydrylation reaction
Aeropyrum pernix
3-Cyano-L-alanine
42% inhibition of the O-acetyl-L-serine sulfhydrylation reaction
Aeropyrum pernix
Cd2+
slightly inhibites both O-acetyl-L-serine sulfhydrylation and O-phospho-L-serine sulfhydrylation
Aeropyrum pernix
CdCl2
25°C, 10 min, 26% inhibition of the O-phospho-L-serine sulfhydrylation reaction, 15% inhibition of the O-acetyl-L-serine sulfhydrylation reaction
Aeropyrum pernix
Co2+
strongly inhibits O-acetyl-L-serine sulfhydrylation, moderately inhibites O-phospho-L-serine sulfhydrylation
Aeropyrum pernix
CoCl2
25°C, 10 min, 61% inhibition of the O-phospho-L-serine sulfhydrylation reaction, 98.8% inhibition of the O-acetyl-L-serine sulfhydrylation reaction
Aeropyrum pernix
Cu2+
strongly inhibits O-acetyl-L-serine sulfhydrylation, moderately inhibites O-phospho-L-serine sulfhydrylation
Aeropyrum pernix
CuCl2
25°C, 10 min, 79% inhibition of the O-phospho-L-serine sulfhydrylation reaction, 98.7% inhibition of the O-acetyl-L-serine sulfhydrylation reaction
Aeropyrum pernix
Fe2+
slightly inhibites both O-acetyl-L-serine sulfhydrylation and O-phospho-L-serine sulfhydrylation
Aeropyrum pernix
Fe3+
strongly inhibits O-acetyl-L-serine sulfhydrylation, slightly inhibites O-phospho-L-serine sulfhydrylation
Aeropyrum pernix
FeCl2
25°C, 10 min, 20% inhibition of the O-phospho-L-serine sulfhydrylation reaction, 27% inhibition of the O-acetyl-L-serine sulfhydrylation reaction
Aeropyrum pernix
FeCl3
25°C, 10 min, 25% inhibition of the O-phospho-L-serine sulfhydrylation reaction, 96.1% inhibition of the O-acetyl-L-serine sulfhydrylation reaction
Aeropyrum pernix
Hg2+
strongly inhibites both O-acetyl-L-serine sulfhydrylation and O-phospho-L-serine sulfhydrylation
Aeropyrum pernix
HgCl2
25°C, 10 min, 98.3% inhibition of the O-phospho-L-serine sulfhydrylation reaction, 80% inhibition of the O-acetyl-L-serine sulfhydrylation reaction
Aeropyrum pernix
additional information
no inhibition by O-phospho-D-serine, EDTA, 2-mercaptoethanol, DTT, NEM, PCMB, and Gd3+, while Ca2+, K+, Na+, Mn2+, and Mg2+ are poor inhibitors; no inhibition of the O-acetyl-L-serine sulfhydrylation reaction by O-phospho-D-serine
Aeropyrum pernix
Ni2+
strongly inhibits O-acetyl-L-serine sulfhydrylation, slightly inhibites O-phospho-L-serine sulfhydrylation
Aeropyrum pernix
NiCl2
25°C, 10 min, 15% inhibition of the O-phospho-L-serine sulfhydrylation reaction, almost complete inhibition of the O-acetyl-L-serine sulfhydrylation reaction
Aeropyrum pernix
O-benzyl-L-serine
36% inhibition of the O-acetyl-L-serine sulfhydrylation reaction
Aeropyrum pernix
O-tert-butyl-L-serine
49% inhibition of the O-acetyl-L-serine sulfhydrylation reaction
Aeropyrum pernix
Pb(CH3COO)2
25°C, 10 min, 95% inhibition of the O-phospho-L-serine sulfhydrylation reaction, 88% inhibition of the O-acetyl-L-serine sulfhydrylation reaction
Aeropyrum pernix
Pb2+
strongly inhibites both O-acetyl-L-serine sulfhydrylation and O-phospho-L-serine sulfhydrylation
Aeropyrum pernix
Zn2+
slightly inhibites both O-acetyl-L-serine sulfhydrylation and O-phospho-L-serine sulfhydrylation
Aeropyrum pernix
ZnCl2
25°C, 10 min, 23% inhibition of the O-phospho-L-serine sulfhydrylation reaction, 25% inhibition of the O-acetyl-L-serine sulfhydrylation reaction
Aeropyrum pernix
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetics; ping-pong bi-bi mechanism
Aeropyrum pernix
0.25
-
hydrogen sulfide
pH 7.6, 60°C, with O-acetyl-L-serine
Aeropyrum pernix
0.25
-
Sulfide
60°C, O-acetyl-L-serine sulfhydrylation reaction
Aeropyrum pernix
5
-
hydrogen sulfide
pH 7.6, 60°C, with O-phospho-L-serine
Aeropyrum pernix
5
-
Sulfide
60°C, O-phospho-L-serine sulfhydrylation reaction
Aeropyrum pernix
12.5
-
hydrogen sulfide
pH 7.6, 85°C, with O-phospho-L-serine
Aeropyrum pernix
12.5
-
Sulfide
85°C, O-phospho-L-serine sulfhydrylation reaction
Aeropyrum pernix
21
-
O-acetyl-L-serine
60°C; pH 7.6, 60°C
Aeropyrum pernix
200
-
O-phospho-L-serine
60°C; pH 7.6, 60°C
Aeropyrum pernix
250
-
O-phospho-L-serine
85°C; pH 7.6, 85°C
Aeropyrum pernix
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
42000
-
2 * 42000
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
enzyme is involved in L-cysteine biosynthesis, pathway overview
L-cysteine + acetate
-
-
ir
O-phospho-L-serine + hydrogen sulfide
Aeropyrum pernix
enzyme is involved in L-cysteine biosynthesis, pathway overview
L-cysteine + phosphate
-
-
ir
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant OASS
Aeropyrum pernix
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
54.5
-
60°C, O-acetyl-L-serine sulfhydrylation reaction, recombinant OASS
Aeropyrum pernix
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3-chloro-L-alanine + hydrogen sulfide
-
655576
Aeropyrum pernix
?
-
-
-
ir
3-chloro-L-alanine + sulfide
heat-labile substrate, 173% of activity compared with O-acetyl-L-serine as substrate
655576
Aeropyrum pernix
?
-
-
-
?
L-azaserine + hydrogen sulfide
O-phospho-L-serine is a heat-stable substrate
655576
Aeropyrum pernix
?
-
-
-
ir
L-azaserine + sulfide
same activity as with O-acetyl-L-serine as substrate
655576
Aeropyrum pernix
?
-
-
-
?
additional information
L-cysteine biosynthesis
655576
Aeropyrum pernix
?
-
-
-
-
additional information
not: 3-chloro-D-alanine, 3-cyano-L-alanine, O-benzyl-L-serine, O-tert-butyl-L-serine, O-phospho-D-serine, O-succinyl-L-homoserine, L-homoserine
655576
Aeropyrum pernix
?
-
-
-
-
additional information
substrate specificity, no activity with 3-chloro-D-alanine, 3-cyano-L-alanine, O-benzyl-L-serine, O-tert-butyl-L-serine, O-phospho-D-serine, O-succinyl-L-homoserine, and L-homoserine
655576
Aeropyrum pernix
?
-
-
-
-
O-acetyl-L-serine + hydrogen sulfide
enzyme is involved in L-cysteine biosynthesis, pathway overview
655576
Aeropyrum pernix
L-cysteine + acetate
-
-
-
ir
O-acetyl-L-serine + hydrogen sulfide
O-acetyl-L-serine is a heat-labile substrate
655576
Aeropyrum pernix
L-cysteine + acetate
-
-
-
ir
O-acetyl-L-serine + sulfide
heat-labile substrate
655576
Aeropyrum pernix
L-cysteine + acetic acid
-
-
-
?
O-phospho-L-serine + hydrogen sulfide
enzyme is involved in L-cysteine biosynthesis, pathway overview
655576
Aeropyrum pernix
L-cysteine + phosphate
-
-
-
ir
O-phospho-L-serine + hydrogen sulfide
O-phospho-L-serine is a heat-stable substrate
655576
Aeropyrum pernix
L-cysteine + phosphate
-
-
-
ir
O-phospho-L-serine + sulfide
heat-stabile substrate, 219% of activity compared with O-acetyl-L-serine as substrate, best substrate at pH 6.7 and 60°C, formation of an alpha-aminoacrylate intermediate between O-phospho-L-serine and pyridoxal 5’-phosphate
655576
Aeropyrum pernix
L-cysteine + phosphate
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
2 * 42000
Aeropyrum pernix
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
70
-
sulfhydrylation of 3-chloro-L-alanine; with substrate 3-chloro-L-alanine
Aeropyrum pernix
80
-
sulfhydrylation of L-azaserine; with substrate L-azaserine
Aeropyrum pernix
90
-
sulfhydrylation of O-phospho-L-serine; with substrate O-phospho-L-serine
Aeropyrum pernix
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
90
-
50% of maximum activity with 3-chloro-L-alanine as substrate
Aeropyrum pernix
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
156
-
O-acetyl-L-serine
60°C; pH 7.6, 60°C
Aeropyrum pernix
3050
-
O-phospho-L-serine
60°C; pH 7.6, 60°C
Aeropyrum pernix
14000
-
O-phospho-L-serine
85°C; pH 7.6, 85°C
Aeropyrum pernix
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.3
8.1
at 85°C; dependent on the substrate, 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
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