BRENDA - Enzyme Database
show all sequences of 2.5.1.65

O-Phospho-l-serine and the thiocarboxylated sulfur carrier protein CysO-COSH are substrates for CysM, a cysteine synthase from Mycobacterium tuberculosis

OLeary, S.E.; Jurgenson, C.T.; Ealick, S.E.; Begley, T.P.; Biochemistry 47, 11606-11615 (2008)

Data extracted from this reference:

Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Mycobacterium tuberculosis
-
isoform CysM
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
specificity of CysM for its amino acid substrate is more than 500-fold greater for O-phospho-L-serine than for O-acetyl-L-serine. Specificity of CysM for this physiological sulfide equivalent, sulfur carrier protein CysO-COSH, is more than 3 orders of magnitude greater than that for bisulfide. CysM active site with the bound aminoacrylate intermediate is protected from solvent and that binding of CysO-COSH produces a conformational change allowing rapid sulfur transfer
685195
Mycobacterium tuberculosis
?
-
-
-
-
O-acetyl-L-serine + hydrogen sulfide
-
685195
Mycobacterium tuberculosis
L-cysteine + acetate
-
-
-
-
O3-phospho-L-serine + hydrogen sulfide
-
685195
Mycobacterium tuberculosis
L-cysteine + phosphate
-
-
-
?
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.025
-
O3-acetyl-L-serine
formation of the aminoacrylate intermediate
Mycobacterium tuberculosis
17
-
O3-phospho-L-serine
formation of the aminoacrylate intermediate
Mycobacterium tuberculosis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
specificity of CysM for its amino acid substrate is more than 500-fold greater for O-phospho-L-serine than for O-acetyl-L-serine. Specificity of CysM for this physiological sulfide equivalent, sulfur carrier protein CysO-COSH, is more than 3 orders of magnitude greater than that for bisulfide. CysM active site with the bound aminoacrylate intermediate is protected from solvent and that binding of CysO-COSH produces a conformational change allowing rapid sulfur transfer
685195
Mycobacterium tuberculosis
?
-
-
-
-
O-acetyl-L-serine + hydrogen sulfide
-
685195
Mycobacterium tuberculosis
L-cysteine + acetate
-
-
-
-
O3-phospho-L-serine + hydrogen sulfide
-
685195
Mycobacterium tuberculosis
L-cysteine + phosphate
-
-
-
?
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.025
-
O3-acetyl-L-serine
formation of the aminoacrylate intermediate
Mycobacterium tuberculosis
17
-
O3-phospho-L-serine
formation of the aminoacrylate intermediate
Mycobacterium tuberculosis
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
-
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-
2
-
5
-
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1
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10
-
1
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7
1
-
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1
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1
1
1
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4
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2
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-
-
10
-
1
-
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7
1
-
-
-
-
1
1
-
7
7
737868
Nakamura
Thermostability and reactivity ...
Aeropyrum pernix, Aeropyrum pernix DSM 11879
Biosci. Biotechnol. Biochem.
79
1280-1286
2015
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-
1
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2
2
6
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1
1
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1
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1
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1
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1
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1
1
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2
2
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1
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6
-
1
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1
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1
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1
1
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738534
Steiner
CysK2 from Mycobacterium tuber ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
J. Bacteriol.
196
3410-3420
2014
-
-
1
-
2
-
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8
-
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2
-
3
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1
1
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6
1
1
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4
2
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1
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1
1
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2
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8
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2
-
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-
1
-
-
-
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6
1
1
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-
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
-
-
-
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-
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-
4
-
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-
1
-
2
-
-
-
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-
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-
1
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-
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1
1
1
11
-
-
-
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-
-
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-
-
-
-
-
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-
1
-
2
-
-
-
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-
-
-
-
-
-
-
-
-
-
-
685195
OLeary
O-Phospho-l-serine and the thi ...
Mycobacterium tuberculosis
Biochemistry
47
11606-11615
2008
-
-
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1
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3
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2
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-
3
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2
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687773
Agren
Cysteine synthase (CYSM) of My ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
J. Biol. Chem.
283
31567-31574
2008
-
-
1
1
1
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4
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6
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1
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8
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1
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1
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2
2
2
2
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4
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1
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8
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1
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702213
Jurgenson
Crystal structure of a sulfur ...
Mycobacterium tuberculosis
Biochemistry
47
10354-10364
2008
-
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1
1
1
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1
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1
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1
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1
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1
1
1
1
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1
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1
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659728
Oda
Three-dimensional structure of ...
Aeropyrum pernix
J. Mol. Biol.
351
334-344
2005
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-
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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1
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1
1
1
1
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1
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1
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4
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1
1
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637385
Mino
Characterization of a novel th ...
Aeropyrum pernix
J. Bacteriol.
185
2277-2284
2003
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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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2
1
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4
1
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1
1
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3
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2
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
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654085
Mino
Crystallization and preliminar ...
Aeropyrum pernix
Acta Crystallogr. Sect. D
59
338-340
2003
-
-
1
1
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3
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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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1
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1
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655576
Mino
A novel O-phospho-L-serine sul ...
Aeropyrum pernix
FEBS Lett.
551
133-138
2003
1
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1
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23
10
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1
3
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1
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1
1
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1
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13
1
3
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1
3
1
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1
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1
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1
1
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23
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10
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1
3
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1
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1
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13
1
3
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3
1
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