BRENDA - Enzyme Database
show all sequences of 2.5.1.65

Characterization of a novel thermostable O-acetylserine sulfhydrylase from Aeropyrum pernix K1

Mino, K.; Ishikawa, K.; J. Bacteriol. 185, 2277-2284 (2003)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli Rosetta (DE3), sequencing
Aeropyrum pernix
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
-
Aeropyrum pernix
0.2
-
Sulfide
below, pH 6.7
Aeropyrum pernix
28
-
O-acetyl-L-serine
pH 6.7
Aeropyrum pernix
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
42000
-
2 * 42000, SDS-PAGE
Aeropyrum pernix
70580
-
sedimentation equilibrium ultracentrifugation
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
biosynthesis of L-cysteine
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Aeropyrum pernix
-
-
-
Purification (Commentary)
Commentary
Organism
recombinant OASS
Aeropyrum pernix
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
50.9
-
pH 6.7, 60°C, O-acetyl-L-serine sulfhydrylation
Aeropyrum pernix
Storage Stability
Storage Stability
Organism
4°C, enzyme solution, stable
Aeropyrum pernix
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-cysteine + dithiothreitol
OASS has a high activity in the L-cysteine desulfurization reaction
637385
Aeropyrum pernix
S-(2,3-hydroxy-4-thiobutyl)-L-cysteine + sulfide
-
-
-
?
additional information
biosynthesis of L-cysteine
637385
Aeropyrum pernix
?
-
-
-
-
additional information
enzyme with cystathionine beta-synthase and O-acetylserine sulfhydrylase activity in vitro, OASS has also L-serine sulfhydrylation and S-sulfo-L-cysteine synthesis activity
637385
Aeropyrum pernix
?
-
-
-
-
O-acetyl-L-serine + sulfide
-
637385
Aeropyrum pernix
L-cysteine + acetic acid
-
-
-
?
Subunits
Subunits
Commentary
Organism
dimer
2 * 42000, SDS-PAGE
Aeropyrum pernix
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
100
-
6 h, pH 6.1 and 6.7: 10% loss of activity, pH 7.5: 44% loss of activity, pH 8.5: 89% loss of activity
Aeropyrum pernix
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
-
Aeropyrum pernix
202
-
O-acetyl-L-serine
pH 6.7
Aeropyrum pernix
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.7
-
-
Aeropyrum pernix
pH Stability
pH Stability
pH Stability Maximum
Commentary
Organism
6.1
-
6 h, 100°C, 10% loss of activity
Aeropyrum pernix
6.7
-
6 h, 100°C, 10% loss of activity
Aeropyrum pernix
7.5
-
6 h, 100°C, 44% loss of activity
Aeropyrum pernix
8.5
-
6 h, 100°C, 89% loss of activity
Aeropyrum pernix
Cofactor
Cofactor
Commentary
Organism
Structure
pyridoxal 5'-phosphate
OASS contains 1.2 molecules pyridoxal 5'-phosphate per subunit, enzyme forms a Schiff base with pyridoxal 5'-phosphate
Aeropyrum pernix
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli Rosetta (DE3), sequencing
Aeropyrum pernix
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
pyridoxal 5'-phosphate
OASS contains 1.2 molecules pyridoxal 5'-phosphate per subunit, enzyme forms a Schiff base with pyridoxal 5'-phosphate
Aeropyrum pernix
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
-
Aeropyrum pernix
0.2
-
Sulfide
below, pH 6.7
Aeropyrum pernix
28
-
O-acetyl-L-serine
pH 6.7
Aeropyrum pernix
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
42000
-
2 * 42000, SDS-PAGE
Aeropyrum pernix
70580
-
sedimentation equilibrium ultracentrifugation
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
biosynthesis of L-cysteine
?
-
-
-
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
50.9
-
pH 6.7, 60°C, O-acetyl-L-serine sulfhydrylation
Aeropyrum pernix
Storage Stability (protein specific)
Storage Stability
Organism
4°C, enzyme solution, stable
Aeropyrum pernix
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-cysteine + dithiothreitol
OASS has a high activity in the L-cysteine desulfurization reaction
637385
Aeropyrum pernix
S-(2,3-hydroxy-4-thiobutyl)-L-cysteine + sulfide
-
-
-
?
additional information
biosynthesis of L-cysteine
637385
Aeropyrum pernix
?
-
-
-
-
additional information
enzyme with cystathionine beta-synthase and O-acetylserine sulfhydrylase activity in vitro, OASS has also L-serine sulfhydrylation and S-sulfo-L-cysteine synthesis activity
637385
Aeropyrum pernix
?
-
-
-
-
O-acetyl-L-serine + sulfide
-
637385
Aeropyrum pernix
L-cysteine + acetic acid
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
2 * 42000, SDS-PAGE
Aeropyrum pernix
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
100
-
6 h, pH 6.1 and 6.7: 10% loss of activity, pH 7.5: 44% loss of activity, pH 8.5: 89% loss of activity
Aeropyrum pernix
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
-
Aeropyrum pernix
202
-
O-acetyl-L-serine
pH 6.7
Aeropyrum pernix
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.7
-
-
Aeropyrum pernix
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
Organism
6.1
-
6 h, 100°C, 10% loss of activity
Aeropyrum pernix
6.7
-
6 h, 100°C, 10% loss of activity
Aeropyrum pernix
7.5
-
6 h, 100°C, 44% loss of activity
Aeropyrum pernix
8.5
-
6 h, 100°C, 89% loss of activity
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
-
-
4
-
-
-
2
-
5
-
-
-
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
-
-
-
-
-
-
-
-
3
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
1
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
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
-
-
-
-
3
-
-
2
1
-
1
-
-
1
-
-
-
1
1
4
1
-
-
1
2
1
-
4
1
-
-
-
-
-
1
1
-
-
-
-
-
-
3
-
-
2
1
-
-
-
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
-
-
-
-
-
-
-
-
-