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1.8.1.12: trypanothione-disulfide reductase

This is an abbreviated version!
For detailed information about trypanothione-disulfide reductase, go to the full flat file.

Word Map on EC 1.8.1.12

Reaction

trypanothione
+
NADP+
=
trypanothione disulfide
 +
NADPH
 +
H+

Synonyms

EC 1.6.4.8, LbTryR, LdTryR, Li-TryR, LiTR, N(1),N(8)-bis(glutathionyl)spermidine reductase, NADPH2:trypanothione oxidoreductase, TbTR, TCDM_11669, TcTR, TPR, TR, trypanothione disulfide reductase, trypanothione reductase, trypanothione-disulfide reductase, TryR

ECTree

     1 Oxidoreductases
         1.8 Acting on a sulfur group of donors
             1.8.1 With NAD+ or NADP+ as acceptor
                1.8.1.12 trypanothione-disulfide reductase

Engineering

Engineering on EC 1.8.1.12 - trypanothione-disulfide reductase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A34E/R37W
-
glutathione reductase mutant, activity switches to trypanothione reductase, termed GRTR, 700fold more activity with trypanothione disulfide than with glutathione
E436A
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
Q439A
the mutant shows slightly increased catalytic efficiency compared to the wild type enzyme
W81A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E201D
-
by site-directed mutagenesis, 5% reductive activity and 50fold increased oxidative activity both compared to wild-type, enhanced quinone reductase activity
E201Q
-
by site-directed mutagenesis, 5% reductive activity and 50fold increased oxidative activity both compared to wild-type, enhanced quinone reductase activity
C53A
-
site-directed mutagenesis, without catalytic active cysteine residue in the active center, no activity with trypanothione disulfide and NADPH, but showing transhydrogenase activity between NADPH and thio-NADP+
C53S
-
site-directed mutagenesis, without catalytic active cysteine residue in the active center, no activity with trypanothione disulfide and NADPH, but showing transhydrogenase activity between NADPH and thio-NADP+
C58S
-
site-directed mutagenesis, without catalytic active cysteine residue in the active center, no activity with trypanothione disulfide and NADPH, but showing transhydrogenase activity between NADPH and thio-NADP+
C53A
-
site-directed mutagenesis, without catalytic active cysteine residue in the active center, no activity with trypanothione disulfide and NADPH, but showing transhydrogenase activity between NADPH and thio-NADP+
-
C53S
-
site-directed mutagenesis, without catalytic active cysteine residue in the active center, no activity with trypanothione disulfide and NADPH, but showing transhydrogenase activity between NADPH and thio-NADP+
-
C58S
-
site-directed mutagenesis, without catalytic active cysteine residue in the active center, no activity with trypanothione disulfide and NADPH, but showing transhydrogenase activity between NADPH and thio-NADP+
-