BRENDA - Enzyme Database show
show all sequences of 6.3.1.8

Purification of glutathionylspermidine and trypanothione synthetase from Crithidia fasciculata

Smith, K.; Nadeau, K.; Bradley, M.; Walsh, C.; Fairlamb, A.H.; Protein Sci. 1, 874-883 (1992)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
reduced trypanothione
-
Crithidia fasciculata
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
90000
-
x * 90000, SDS-PAGE
Crithidia fasciculata
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
gamma-L-Glutamyl-L-cysteinyl-glycine + spermidine + ATP
Crithidia fasciculata
the enzyme is involved in the biosynthesis of the trypanosomatid-specific dithiol trypanothione
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Crithidia fasciculata
-
-
-
Purification (Commentary)
Commentary
Organism
-
Crithidia fasciculata
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
-
Crithidia fasciculata
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
gamma-L-Glu-L-Cys-Gly + spermidine + ATP
-
964
Crithidia fasciculata
N1-(gamma-L-Glu-L-Cys-Gly)-spermidine + ADP + phosphate
-
964
Crithidia fasciculata
-
gamma-L-Glutamyl-L-cysteinyl-glycine + spermidine + ATP
the enzyme is involved in the biosynthesis of the trypanosomatid-specific dithiol trypanothione
964
Crithidia fasciculata
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
?
x * 90000, SDS-PAGE
Crithidia fasciculata
More
in vivo a complex between EC 6.3.1.8 and EC 6.3.1.9 exists that persists during purification
Crithidia fasciculata
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
-
Crithidia fasciculata
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
reduced trypanothione
-
Crithidia fasciculata
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
90000
-
x * 90000, SDS-PAGE
Crithidia fasciculata
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
gamma-L-Glutamyl-L-cysteinyl-glycine + spermidine + ATP
Crithidia fasciculata
the enzyme is involved in the biosynthesis of the trypanosomatid-specific dithiol trypanothione
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
-
Crithidia fasciculata
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
-
Crithidia fasciculata
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
gamma-L-Glu-L-Cys-Gly + spermidine + ATP
-
964
Crithidia fasciculata
N1-(gamma-L-Glu-L-Cys-Gly)-spermidine + ADP + phosphate
-
964
Crithidia fasciculata
-
gamma-L-Glutamyl-L-cysteinyl-glycine + spermidine + ATP
the enzyme is involved in the biosynthesis of the trypanosomatid-specific dithiol trypanothione
964
Crithidia fasciculata
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 90000, SDS-PAGE
Crithidia fasciculata
More
in vivo a complex between EC 6.3.1.8 and EC 6.3.1.9 exists that persists during purification
Crithidia fasciculata
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
-
Crithidia fasciculata
Other publictions for EC 6.3.1.8
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)
744964
Sousa
Genetic and chemical analyses ...
Leishmania infantum, Leishmania infantum MHOM / MA / 67 / ITMAP263
Free Radic. Biol. Med.
73
229-238
2014
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6
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727554
Chattopadhyay
Escherichia coli glutathionyls ...
Escherichia coli K-12
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338
132-140
2013
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727627
Sui
Comparison of the functions of ...
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Int. J. Biochem. Mol. Biol.
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302-312
2012
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716863
Pai
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20
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2011
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712459
Chiang
Protein S-thiolation by Glutat ...
Escherichia coli
J. Biol. Chem.
285
25345-25353
2010
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692316
Oza
ATP-dependent ligases in trypa ...
Crithidia fasciculata
FEBS J.
275
5408-5421
2008
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1
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4
3
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1
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7
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3
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1
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4
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4
4
3
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3
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1
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1
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673330
Pai
Dual binding sites for translo ...
Escherichia coli
EMBO J.
25
5970-5982
2006
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1
1
10
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4
19
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1
2
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4
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1
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1
1
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1
2
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1
1
1
10
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4
2
19
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1
2
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1
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1
1
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661011
Ariyanayagam
Phenotypic analysis of trypano ...
Trypanosoma brucei
Biochem. J.
391
425-432
2005
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1
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1
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1
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662446
Comini
Trypanothione synthesis in Cri ...
Crithidia fasciculata
J. Biol. Chem.
280
6850-6860
2005
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3
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1
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3
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6
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5
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3
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1
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5
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1
2
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662802
Oza
Trypanothione biosynthesis in ...
Leishmania major
Mol. Biochem. Parasitol.
139
107-116
2005
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1
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5
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661810
Comini
Valdiation of Trypanosoma bruc ...
Trypanosoma brucei
Free Radic. Biol. Med.
36
1289-1302
2004
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1
1
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1
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7
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1
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1
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649733
Oza
Characterization of recombinan ...
Crithidia fasciculata
Biochem. J.
364
679-686
2002
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1
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1
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7
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3
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3
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650561
Amssoms
Glutathione-like tripeptides a ...
Crithidia fasciculata
Bioorg. Med. Chem. Lett.
12
2703-2705
2002
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2
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965
Tetaud
Cloning and characterization o ...
Crithidia fasciculata
J. Biol. Chem.
273
19383-19390
1998
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7
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966
De Craecker
Characterization of the peptid ...
Crithidia fasciculata
Mol. Biochem. Parasitol.
84
25-32
1997
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13
8
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2
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1
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11
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8
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13
1
8
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11
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8
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967
Lin
Aldehyde and phosphinate analo ...
Escherichia coli
Chem. Biol.
4
859-866
1997
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968
Chen
Design, synthesis, and biochem ...
Escherichia coli
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40
3842-3850
1997
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963
Nadeau
-
Biochemical studies on protein ...
Crithidia fasciculata
Diss. Abstr. Int. B
56
3744
1995
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969
Bollinger
Glutathionylspermidine metabol ...
Escherichia coli
J. Biol. Chem.
270
14031-14041
1995
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964
Smith
Purification of glutathionylsp ...
Crithidia fasciculata
Protein Sci.
1
874-883
1992
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962
Tabor
-
Glutathionylspermidine synthet ...
Escherichia coli
Methods Enzymol.
17
815-817
1971
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