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Literature summary extracted from

  • Arias, D.G.; Marquez, V.E.; Beccaria, A.J.; Guerrero, S.A.; Iglesias, A.A.
    Purification and characterization of a glutathione reductase from Phaeodactylum tricornutum (2010), Protist, 161, 91-101.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.8.1.7 Co2+ GRase-1 is moderately sensitive to inhibition by Co2+ Phaeodactylum tricornutum
1.8.1.7 Cu2+ GRase-1 is very sensitive to inhibition by Cu2+ Phaeodactylum tricornutum
1.8.1.7 glutathione GSH functions as an inhibitor at relatively high concentrations (41 mM), and also only in the lower substrate concentration range Phaeodactylum tricornutum
1.8.1.7 NADP+ competitive product inhibition regarding NADPH and non-competitive product inhibition regarding glutathione disulfide, however, NADP+ (up to 1m M) is not inhibitor when assays are performed at 1 mM glutathione disulfide and 300 mM NADPH Phaeodactylum tricornutum
1.8.1.7 Ni2+
-
Phaeodactylum tricornutum
1.8.1.7 Zn2+ GRase-1 is very sensitive to inhibition by Zn2+ Phaeodactylum tricornutum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.8.1.7 0.014
-
NADPH at 30°C and pH 7.5 Phaeodactylum tricornutum
1.8.1.7 0.06
-
glutathione disulfide at 30°C and pH 7.5 Phaeodactylum tricornutum

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.8.1.7 40000
-
composed of two major proteins of 58000 and 40000 Da, SDS-PAGE Phaeodactylum tricornutum
1.8.1.7 53470
-
subunit, calculated from amino acid sequence Phaeodactylum tricornutum
1.8.1.7 58000
-
composed of two major proteins of 58000 and 40000 Da, SDS-PAGE Phaeodactylum tricornutum
1.8.1.7 59000
-
2 * 59000, native PAGE Phaeodactylum tricornutum
1.8.1.7 118000
-
native molecular mass, native PAGE Phaeodactylum tricornutum

Organism

EC Number Organism UniProt Comment Textmining
1.8.1.7 Phaeodactylum tricornutum
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.8.1.7 ammonium sulfate precipitation, DEAE-Sepharose column chromatography, Blue-A Sepharose column chromatography, and 2',5'-ADP-Sepharose column chromatography Phaeodactylum tricornutum

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.8.1.7 0.46
-
enzyme from soluble extract, at 30°C and pH 7.5 Phaeodactylum tricornutum
1.8.1.7 73.3
-
after 161fold purification, at 30°C and pH 7.5 Phaeodactylum tricornutum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.1.7 glutathione disulfide + NADPH + H+
-
Phaeodactylum tricornutum glutathione + NADP+ using levels up to 300 mM NADP+ and 1 mM glutathione, the enzyme does not catalyse the reverse reaction, indicating that its physiological function is the reduction of GSSG or GSNO but not the opposite ir
1.8.1.7 additional information the enzyme is not effective to reduce cystine, lipoamide, nor trypanothione disulfide Phaeodactylum tricornutum ?
-
?

Subunits

EC Number Subunits Comment Organism
1.8.1.7 homodimer 2 * 59000, native PAGE Phaeodactylum tricornutum

Synonyms

EC Number Synonyms Comment Organism
1.8.1.7 glutathione reductase
-
Phaeodactylum tricornutum
1.8.1.7 glutathione:NADP+ oxidoreductase
-
Phaeodactylum tricornutum
1.8.1.7 GRase-1
-
Phaeodactylum tricornutum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.8.1.7 35
-
-
Phaeodactylum tricornutum

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.8.1.7 30 35 the abrupt decrease in activity observed at temperatures higher than 35°C, can be associated with loss of enzyme stability beyond 30°C Phaeodactylum tricornutum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.8.1.7 8
-
-
Phaeodactylum tricornutum

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.8.1.7 6.5 10 in 100 mM Tris-HCl buffer Phaeodactylum tricornutum

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.8.1.7 6.5 10 the enzyme remains stable in 100 mM Tris-HCl buffer between pH 6.5 and 10.0, the activity remains practically unchanged between pH 6.5-7.5 and decreases significantly only above pH 8.5 Phaeodactylum tricornutum

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.1.7 NADPH utilizes NADPH but not NADH as electron donor Phaeodactylum tricornutum

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.8.1.7 0.052
-
NADP+ competitive product inhibition regarding NADPH, at 30°C and pH 7.5 Phaeodactylum tricornutum
1.8.1.7 1
-
NADP+ non-competitive product inhibition regarding glutathione disulfide, at 30°C and pH 7.5 Phaeodactylum tricornutum
1.8.1.7 5
-
glutathione competitive product inhibition regarding glutathione disulfide, at 30°C and pH 7.5 Phaeodactylum tricornutum
1.8.1.7 10
-
glutathione non-competitive product inhibition regarding NADPH, at 30°C and pH 7.5 Phaeodactylum tricornutum

pI Value

EC Number Organism Comment pI Value Maximum pI Value
1.8.1.7 Phaeodactylum tricornutum calculated from amino acid sequence
-
5

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
1.8.1.7 0.0034
-
at 30°C and pH 7.5 Phaeodactylum tricornutum Cu2+
1.8.1.7 0.0042
-
at 30°C and pH 7.5 Phaeodactylum tricornutum Zn2+
1.8.1.7 0.036
-
at 30°C and pH 7.5 Phaeodactylum tricornutum Co2+
1.8.1.7 0.534
-
at 30°C and pH 7.5 Phaeodactylum tricornutum Ni2+

General Information

EC Number General Information Comment Organism
1.8.1.7 physiological function the enzyme's physiological function is the reduction of glutathione disulfide or GSNO but not the opposite Phaeodactylum tricornutum