DB code: T00242
| CATH domain | 3.50.50.60 : FAD/NAD(P)-binding domain | Catalytic domain |
|---|---|---|
| 3.50.50.60 : FAD/NAD(P)-binding domain | Catalytic domain | |
| 3.30.390.30 : Enolase-like; domain 1 | Catalytic domain | |
| E.C. | 1.8.1.12 | |
| CSA | ||
| M-CSA | ||
| MACiE | ||
| CATH domain | Related DB codes (homologues) |
|---|---|
| 3.30.390.30 : Enolase-like; domain 1 | M00163 T00017 T00213 T00233 |
| 3.50.50.60 : FAD/NAD(P)-binding domain | M00163 D00015 D00041 D00042 D00045 D00064 D00071 T00004 T00015 T00017 T00025 T00211 T00213 T00233 |
| Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | Pfam |
|---|---|---|---|
| P39040 |
Trypanothione reductase (TR) (EC 1.8.1.12) (N(1),N
|
8)-bis(glutathionyl)spermidine reductase
|
PF00070
(Pyr_redox)
PF07992 (Pyr_redox_2) PF02852 (Pyr_redox_dim) [Graphical View] |
| P28593 |
Trypanothione reductase (TR) (EC 1.8.1.12) (N(1),N
|
8)-bis(glutathionyl)spermidine reductase
|
PF00070
(Pyr_redox)
PF07992 (Pyr_redox_2) PF02852 (Pyr_redox_dim) [Graphical View] |
| KEGG enzyme name |
|---|
|
trypanothione-disulfide reductase
trypanothione reductase NADPH2:trypanothione oxidoreductase |
| UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
|---|---|---|---|---|---|
| P39040 | TYTR_CRIFA | Trypanothione + NADP(+) = trypanothione disulfide + NADPH. | Homodimer. | Cytoplasm. | Binds 1 FAD per subunit. |
| P28593 | TYTR_TRYCR | Trypanothione + NADP(+) = trypanothione disulfide + NADPH. | Homodimer. | Cytoplasm. | Binds 1 FAD per subunit. |
| KEGG Pathways | Map code | Pathways | E.C. |
|---|---|---|
| MAP00480 | Glutathione metabolism |
| Compound table | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Cofactors | Substrates | Products | Intermediates | |||||||||
| KEGG-id | C00016 | C00005 | C03170 | C00080 | C00006 | C02090 | ||||||
| E.C. |
(disulfide bonded)
|
|||||||||||
| Compound | FAD | NADPH | Oxidized trypanothione | H+ | NADP+ | Trypanothione | Enzyme-Trypanothine complex | |||||
| Type | amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,nucleotide | amide group,amine group,nucleotide | amino acids,amine group,disulfide bond,lipid,peptide/protein | others | amide group,amine group,nucleotide | amino acids,amine group,lipid,peptide/protein,sulfhydryl group | ||||||
| ChEBI |
16238 16238 |
16474 16474 |
35490 35490 |
15378 15378 |
18009 18009 |
17842 17842 |
||||||
| PubChem |
643975 643975 |
5884 5884 |
115098 115098 |
1038 1038 |
5886 5886 |
449517 449517 |
||||||
| 1aogA01 |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Unbound | ||
| 1aogB01 |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Unbound | ||
| 1bzlA01 |
|
|
|
|
|
Bound:FAD | Unbound | Bound:GCG | Unbound | Unbound | ||
| 1bzlB01 |
|
|
|
|
|
Bound:FAD | Unbound | Bound:GCG | Unbound | Unbound | ||
| 1feaA01 |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Unbound | ||
| 1feaB01 |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Unbound | ||
| 1feaC01 |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Unbound | ||
| 1feaD01 |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Unbound | ||
| 1febA01 |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Unbound | ||
| 1febB01 |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Unbound | ||
| 1fecA01 |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Unbound | ||
| 1fecB01 |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Unbound | ||
| 1gxfA01 |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:QUM_502 | |
| 1gxfB01 |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:QUM_502 | |
| 1ndaA01 |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Unbound | ||
| 1ndaB01 |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Unbound | ||
| 1ndaC01 |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Unbound | ||
| 1ndaD01 |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Unbound | ||
| 1typA01 |
|
|
|
|
|
Bound:FAD | Unbound | Analogue:SPD-GSH-GSH-SPD | Unbound | Unbound | ||
| 1typB01 |
|
|
|
|
|
Bound:FAD | Unbound | Analogue:SPD-GSH-GSH-SPD | Unbound | Unbound | ||
| 1tytA01 |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Unbound | ||
| 1tytB01 |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Unbound | ||
| 2tprA01 |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Unbound | ||
| 2tprB01 |
|
|
|
|
|
Bound:FAD | Unbound | Unbound | Unbound | Unbound | ||
| 1aogA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1aogB02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1bzlA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1bzlB02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1feaA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1feaB02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1feaC02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1feaD02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1febA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1febB02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1fecA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1fecB02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1gxfA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1gxfB02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1ndaA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1ndaB02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1ndaC02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1ndaD02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1typA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Bound:NAP | Unbound | ||
| 1typB02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Bound:NAP | Unbound | ||
| 1tytA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1tytB02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 2tprA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 2tprB02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1aogA03 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1aogB03 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1bzlA03 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1bzlB03 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1feaA03 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1feaB03 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1feaC03 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1feaD03 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1febA03 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1febB03 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1fecA03 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1fecB03 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1gxfA03 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1gxfB03 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1ndaA03 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1ndaB03 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1ndaC03 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1ndaD03 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1typA03 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1typB03 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1tytA03 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1tytB03 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 2tprA03 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 2tprB03 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | ||
| Reference for Active-site residues | ||
|---|---|---|
| resource | references | E.C. |
| Swiss-prot;P39040, P28593 & literature [7], [16], [23] | ||
| Active-site residues | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
| 1aogA01 |
|
|
|
|
|
CYS 53;CYS 58;LYS 61 | disulfide bonded/oxidized form C53-C58 | |||
| 1aogB01 |
|
|
|
|
|
CYS 53;CYS 58;LYS 61 | disulfide bonded/oxidized form C53-C58 | |||
| 1bzlA01 |
|
|
|
|
|
CYS 53;CYS 58;LYS 61 | disulfide bonded/oxidized form C53-C58 | |||
| 1bzlB01 |
|
|
|
|
|
CYS 53;CYS 58;LYS 61 | disulfide bonded/oxidized form C53-C58 | |||
| 1feaA01 |
|
|
|
|
|
CYS 51;CYS 56;LYS 59 | disulfide bonded/oxidized form C51-C56 | |||
| 1feaB01 |
|
|
|
|
|
CYS 51;CYS 56;LYS 59 | disulfide bonded/oxidized form C51-C56 | |||
| 1feaC01 |
|
|
|
|
|
CYS 51;CYS 56;LYS 59 | disulfide bonded/oxidized form C51-C56 | |||
| 1feaD01 |
|
|
|
|
|
CYS 51;CYS 56;LYS 59 | disulfide bonded/oxidized form C51-C56 | |||
| 1febA01 |
|
|
|
|
|
CYS 51;CYS 56;LYS 59 | disulfide bonded/oxidized form C51-C56 | |||
| 1febB01 |
|
|
|
|
|
CYS 51;CYS 56;LYS 59 | disulfide bonded/oxidized form C51-C56 | |||
| 1fecA01 |
|
|
|
|
|
CYS 51;CYS 56;LYS 59 | disulfide bonded/oxidized form C51-C56 | |||
| 1fecB01 |
|
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|
|
|
CYS 51;CYS 56;LYS 59 | disulfide bonded/oxidized form C51-C56 | |||
| 1gxfA01 |
|
|
|
|
|
CYS 53;CYS 58;LYS 61 | reduced form C53, C58 | |||
| 1gxfB01 |
|
|
|
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|
CYS 53;CYS 58;LYS 61 | reduced form C53, C58 | |||
| 1ndaA01 |
|
|
|
|
|
CYS 52;CYS 57;LYS 60 | disulfide bonded/oxidized form C52-C57 | |||
| 1ndaB01 |
|
|
|
|
|
CYS 52;CYS 57;LYS 60 | disulfide bonded/oxidized form C52-C57 | |||
| 1ndaC01 |
|
|
|
|
|
CYS 52;CYS 57;LYS 60 | disulfide bonded/oxidized form C52-C57 | |||
| 1ndaD01 |
|
|
|
|
|
CYS 52;CYS 57;LYS 60 | disulfide bonded/oxidized form C52-C57 | |||
| 1typA01 |
|
|
|
|
|
CYS 52;CYS 57;LYS 60 | disulfide bonded/oxidized form C52-C57 | |||
| 1typB01 |
|
|
|
|
|
CYS 52;CYS 57;LYS 60 | disulfide bonded/oxidized form C52-C57 | |||
| 1tytA01 |
|
|
|
|
|
CYS 52;CYS 57;LYS 60 | disulfide bonded/oxidized form C52-C57 | |||
| 1tytB01 |
|
|
|
|
|
CYS 52;CYS 57;LYS 60 | disulfide bonded/oxidized form C52-C57 | |||
| 2tprA01 |
|
|
|
|
|
CYS 51;CYS 56;LYS 59 | disulfide bonded/oxidized form C51-C56 | |||
| 2tprB01 |
|
|
|
|
|
CYS 51;CYS 56;LYS 59 | disulfide bonded/oxidized form C51-C56 | |||
| 1aogA02 |
|
|
|
|
|
GLU 203 | ||||
| 1aogB02 |
|
|
|
|
|
GLU 203 | ||||
| 1bzlA02 |
|
|
|
|
|
GLU 203 | ||||
| 1bzlB02 |
|
|
|
|
|
GLU 203 | ||||
| 1feaA02 |
|
|
|
|
|
GLU 201 | ||||
| 1feaB02 |
|
|
|
|
|
GLU 201 | ||||
| 1feaC02 |
|
|
|
|
|
GLU 201 | ||||
| 1feaD02 |
|
|
|
|
|
GLU 201 | ||||
| 1febA02 |
|
|
|
|
|
GLU 201 | ||||
| 1febB02 |
|
|
|
|
|
GLU 201 | ||||
| 1fecA02 |
|
|
|
|
|
GLU 201 | ||||
| 1fecB02 |
|
|
|
|
|
GLU 201 | ||||
| 1gxfA02 |
|
|
|
|
|
GLU 203 | ||||
| 1gxfB02 |
|
|
|
|
|
GLU 203 | ||||
| 1ndaA02 |
|
|
|
|
|
GLU 202 | ||||
| 1ndaB02 |
|
|
|
|
|
GLU 202 | ||||
| 1ndaC02 |
|
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|
|
|
GLU 202 | ||||
| 1ndaD02 |
|
|
|
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|
GLU 202 | ||||
| 1typA02 |
|
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|
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|
GLU 202 | ||||
| 1typB02 |
|
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|
GLU 202 | ||||
| 1tytA02 |
|
|
|
|
|
GLU 202 | ||||
| 1tytB02 |
|
|
|
|
|
GLU 202 | ||||
| 2tprA02 |
|
|
|
|
|
GLU 201 | ||||
| 2tprB02 |
|
|
|
|
|
GLU 201 | ||||
| 1aogA03 |
|
|
|
|
|
HIS 461;GLU 466 | ||||
| 1aogB03 |
|
|
|
|
|
HIS 461;GLU 466 | ||||
| 1bzlA03 |
|
|
|
|
|
HIS 461;GLU 466 | ||||
| 1bzlB03 |
|
|
|
|
|
HIS 461;GLU 466 | ||||
| 1feaA03 |
|
|
|
|
|
HIS 460;GLU 465 | ||||
| 1feaB03 |
|
|
|
|
|
HIS 460;GLU 465 | ||||
| 1feaC03 |
|
|
|
|
|
HIS 460;GLU 465 | ||||
| 1feaD03 |
|
|
|
|
|
HIS 460;GLU 465 | ||||
| 1febA03 |
|
|
|
|
|
HIS 460;GLU 465 | ||||
| 1febB03 |
|
|
|
|
|
HIS 460;GLU 465 | ||||
| 1fecA03 |
|
|
|
|
|
HIS 460;GLU 465 | ||||
| 1fecB03 |
|
|
|
|
|
HIS 460;GLU 465 | ||||
| 1gxfA03 |
|
|
|
|
|
HIS 461;GLU 466 | ||||
| 1gxfB03 |
|
|
|
|
|
HIS 461;GLU 466 | ||||
| 1ndaA03 |
|
|
|
|
|
HIS 460;GLU 465 | ||||
| 1ndaB03 |
|
|
|
|
|
HIS 460;GLU 465 | ||||
| 1ndaC03 |
|
|
|
|
|
HIS 460;GLU 465 | ||||
| 1ndaD03 |
|
|
|
|
|
HIS 460;GLU 465 | ||||
| 1typA03 |
|
|
|
|
|
HIS 461;GLU 466 | ||||
| 1typB03 |
|
|
|
|
|
HIS 461;GLU 466 | ||||
| 1tytA03 |
|
|
|
|
|
HIS 461;GLU 466 | ||||
| 1tytB03 |
|
|
|
|
|
HIS 461;GLU 466 | ||||
| 2tprA03 |
|
|
|
|
|
HIS 460;GLU 465 | ||||
| 2tprB03 |
|
|
|
|
|
HIS 460;GLU 465 | ||||
| References for Catalytic Mechanism | ||
|---|---|---|
| References | Sections | No. of steps in catalysis |
|
[1]
|
Fig.1, p.315 | |
|
[5]
|
||
|
[6]
|
p.8766-8767 | |
|
[7]
|
p.329-332 | |
|
[8]
|
p.3092-3094 | |
|
[9]
|
||
|
[12]
|
p.147-151 | |
|
[13]
|
||
|
[15]
|
||
|
[17]
|
p.55-57 | |
|
[23]
|
||
| References | |
|---|---|
| [1] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 2666188 |
| Journal | Biochem Soc Trans |
| Year | 1989 |
| Volume | 17 |
| Pages | 315-7 |
| Authors | Krauth-Siegel RL, Jockers-Scherubl MC, Becker K, Schirmer RH |
| Title | NADPH-dependent disulphide reductases. |
| Related PDB | |
| Related UniProtKB | |
| [2] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 2254926 |
| Journal | J Mol Biol |
| Year | 1990 |
| Volume | 216 |
| Pages | 235-7 |
| Authors | Hunter WN, Smith K, Derewenda Z, Harrop SJ, Habash J, Islam MS, Helliwell JR, Fairlamb AH |
| Title | Initiating a crystallographic study of trypanothione reductase. |
| Related PDB | |
| Related UniProtKB | |
| [3] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 2231707 |
| Journal | J Mol Biol |
| Year | 1990 |
| Volume | 215 |
| Pages | 335-7 |
| Authors | Kuriyan J, Wong L, Guenther BD, Murgolo NJ, Cerami A, Henderson GB |
| Title | Preliminary crystallographic analysis of trypanothione reductase from Crithidia fasciculata. |
| Related PDB | |
| Related UniProtKB | |
| [4] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 2059620 |
| Journal | Biochemistry |
| Year | 1991 |
| Volume | 30 |
| Pages | 6124-7 |
| Authors | Bradley M, Bucheler US, Walsh CT |
| Title | Redox enzyme engineering: conversion of human glutathione reductase into a trypanothione reductase. |
| Related PDB | |
| Related UniProtKB | |
| [5] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 2007114 |
| Journal | Biochemistry |
| Year | 1991 |
| Volume | 30 |
| Pages | 2761-7 |
| Authors | Sullivan FX, Sobolov SB, Bradley M, Walsh CT |
| Title | Mutational analysis of parasite trypanothione reductase: acquisition of glutathione reductase activity in a triple mutant. |
| Related PDB | |
| Related UniProtKB | |
| [6] | |
| Resource | |
| Comments | X-ray crystallography |
| Medline ID | |
| PubMed ID | 1924336 |
| Journal | Proc Natl Acad Sci U S A |
| Year | 1991 |
| Volume | 88 |
| Pages | 8764-8 |
| Authors | Kuriyan J, Kong XP, Krishna TS, Sweet RM, Murgolo NJ, Field H, Cerami A, Henderson GB |
| Title | X-ray structure of trypanothione reductase from Crithidia fasciculata at 2.4-A resolution. |
| Related PDB | 2tpr |
| Related UniProtKB | |
| [7] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) |
| Medline ID | 92395672 |
| PubMed ID | 1522596 |
| Journal | J Mol Biol |
| Year | 1992 |
| Volume | 227 |
| Pages | 322-33 |
| Authors | Hunter WN, Bailey S, Habash J, Harrop SJ, Helliwell JR, Aboagye-Kwarteng T, Smith K, Fairlamb AH |
| Title |
Active site of trypanothione reductase. |
| Related PDB | |
| Related UniProtKB | P39040 |
| [8] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 1453951 |
| Journal | Mol Microbiol |
| Year | 1992 |
| Volume | 6 |
| Pages | 3089-99 |
| Authors | Aboagye-Kwarteng T, Smith K, Fairlamb AH |
| Title | Molecular characterization of the trypanothione reductase gene from Crithidia fasciculata and Trypanosoma brucei: comparison with other flavoprotein disulphide oxidoreductases with respect to substrate specificity and catalytic mechanism. |
| Related PDB | |
| Related UniProtKB | |
| [9] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) |
| Medline ID | 93238745 |
| PubMed ID | 8477734 |
| Journal | Eur J Biochem |
| Year | 1993 |
| Volume | 213 |
| Pages | 67-75 |
| Authors | Bailey S, Smith K, Fairlamb AH, Hunter WN |
| Title | Substrate interactions between trypanothione reductase and N1-glutathionylspermidine disulphide at 0.28-nm resolution. |
| Related PDB | 1typ |
| Related UniProtKB | P39040 |
| [10] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8428618 |
| Journal | FEBS Lett |
| Year | 1993 |
| Volume | 317 |
| Pages | 105-8 |
| Authors | Krauth-Siegel RL, Sticherling C, Jost I, Walsh CT, Pai EF, Kabsch W, Lantwin CB |
| Title |
Crystallization and preliminary crystallographic analysis of trypanothione reductase from Trypanosoma cruzi, |
| Related PDB | |
| Related UniProtKB | |
| [11] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8371273 |
| Journal | J Mol Biol |
| Year | 1993 |
| Volume | 232 |
| Pages | 1217-20 |
| Authors | Zhang Y, Bailey S, Naismith JH, Bond CS, Habash J, McLaughlin P, Papiz MZ, Borges A, Cunningham M, Fairlamb AH, et al |
| Title |
Trypanosoma cruzi trypanothione reductase. |
| Related PDB | |
| Related UniProtKB | |
| [12] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) |
| Medline ID | |
| PubMed ID | |
| Journal | Acta Crystallogr D Biol Crystallogr |
| Year | 1994 |
| Volume | 50 |
| Pages | 139-54 |
| Authors | Bailey S, Fairlamb AH, Hunter WN |
| Title | Structure of trypanothione reductase from Crithidia fasciculata at 2.6-A resolution; enzyme-NADP interactions at 2.8-A resolution |
| Related PDB | 1tyt |
| Related UniProtKB | P39040 |
| [13] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) |
| Medline ID | 94211757 |
| PubMed ID | 8159665 |
| Journal | Proteins |
| Year | 1994 |
| Volume | 18 |
| Pages | 161-73 |
| Authors | Lantwin CB, Schlichting I, Kabsch W, Pai EF, Krauth-Siegel RL |
| Title | The structure of Trypanosoma cruzi trypanothione reductase in the oxidized and NADPH reduced state. |
| Related PDB | |
| Related UniProtKB | P28593 |
| [14] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) |
| Medline ID | |
| PubMed ID | |
| Journal | Acta Crystallogr D Biol Crystallogr |
| Year | 1995 |
| Volume | 51 |
| Pages | 337-41 |
| Authors | Strickland CL, Puchalski R, Savvides SN, Karplus PA |
| Title | Overexpression of Crithidia fasciculata trypanothione reductase and crystallization using a novel geometry. |
| Related PDB | |
| Related UniProtKB | P39040 |
| [15] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 7548022 |
| Journal | Biochemistry |
| Year | 1995 |
| Volume | 34 |
| Pages | 12697-703 |
| Authors | Zheng R, Cenas N, Blanchard JS |
| Title | Catalytic and potentiometric characterization of E201D and E201Q mutants of Trypanosoma congolense trypanothione reductase. |
| Related PDB | |
| Related UniProtKB | |
| [16] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 7672506 |
| Journal | FASEB J |
| Year | 1995 |
| Volume | 9 |
| Pages | 1138-46 |
| Authors | Krauth-Siegel RL, Schoneck R |
| Title |
Flavoprotein structure and mechanism. |
| Related PDB | |
| Related UniProtKB | |
| [17] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) |
| Medline ID | 96367082 |
| PubMed ID | 8771196 |
| Journal | Protein Sci |
| Year | 1996 |
| Volume | 5 |
| Pages | 52-61 |
| Authors | Zhang Y, Bond CS, Bailey S, Cunningham ML, Fairlamb AH, Hunter WN |
| Title | The crystal structure of trypanothione reductase from the human pathogen Trypanosoma cruzi at 2.3 A resolution. |
| Related PDB | 1aog |
| Related UniProtKB | P28593 |
| [18] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8628734 |
| Journal | Proteins |
| Year | 1996 |
| Volume | 24 |
| Pages | 73-80 |
| Authors | Jacoby EM, Schlichting I, Lantwin CB, Kabsch W, Krauth-Siegel RL |
| Title | Crystal structure of the Trypanosoma cruzi trypanothione reductase.mepacrine complex. |
| Related PDB | |
| Related UniProtKB | |
| [19] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9174360 |
| Journal | Biochemistry |
| Year | 1997 |
| Volume | 36 |
| Pages | 6437-47 |
| Authors | Stoll VS, Simpson SJ, Krauth-Siegel RL, Walsh CT, Pai EF |
| Title | Glutathione reductase turned into trypanothione reductase: structural analysis of an engineered change in substrate specificity. |
| Related PDB | |
| Related UniProtKB | |
| [20] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9057833 |
| Journal | Eur J Biochem |
| Year | 1997 |
| Volume | 243 |
| Pages | 690-4 |
| Authors | Marsh IR, Bradley M |
| Title | Substrate specificity of trypanothione reductase. |
| Related PDB | |
| Related UniProtKB | |
| [21] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9309766 |
| Journal | Parasitology |
| Year | 1997 |
| Volume | 114 Suppl |
| Pages | S17-29 |
| Authors | Hunter WN |
| Title | A structure-based approach to drug discovery; crystallography and implications for the development of antiparasite drugs. |
| Related PDB | |
| Related UniProtKB | |
| [22] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9986706 |
| Journal | J Med Chem |
| Year | 1999 |
| Volume | 42 |
| Pages | 364-72 |
| Authors | Gallwitz H, Bonse S, Martinez-Cruz A, Schlichting I, Schumacher K, Krauth-Siegel RL |
| Title |
Ajoene is an inhibitor and subversive substrate of human glutathione reductase and Trypanosoma cruzi trypanothione reductase: crystallographic, |
| Related PDB | |
| Related UniProtKB | |
| [23] | |
| Resource | |
| Comments | X-ray crystallography |
| Medline ID | |
| PubMed ID | 10368274 |
| Journal | Structure Fold Des |
| Year | 1999 |
| Volume | 7 |
| Pages | 81-9 |
| Authors | Bond CS, Zhang Y, Berriman M, Cunningham ML, Fairlamb AH, Hunter WN |
| Title |
Crystal structure of Trypanosoma cruzi trypanothione reductase in complex with trypanothione, |
| Related PDB | 1bzl |
| Related UniProtKB | |
| [24] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10968268 |
| Journal | Bioorg Med Chem |
| Year | 2000 |
| Volume | 8 |
| Pages | 95-103 |
| Authors | Bonnet B, Soullez D, Girault S, Maes L, Landry V, Davioud-Charvet E, Sergheraert C |
| Title | Trypanothione reductase inhibition/trypanocidal activity relationships in a 1,4-bis(3-aminopropyl)piperazine series. |
| Related PDB | |
| Related UniProtKB | |
| [25] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11170645 |
| Journal | J Med Chem |
| Year | 2001 |
| Volume | 44 |
| Pages | 548-65 |
| Authors | Salmon-Chemin L, Buisine E, Yardley V, Kohler S, Debreu MA, Landry V, Sergheraert C, Croft SL, Krauth-Siegel RL, Davioud-Charvet E |
| Title | 2- and 3-substituted 1,4-naphthoquinone derivatives as subversive substrates of trypanothione reductase and lipoamide dehydrogenase from Trypanosoma cruzi: synthesis and correlation between redox cycling activities and in vitro cytotoxicity. |
| Related PDB | |
| Related UniProtKB | |
| [26] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11867629 |
| Journal | J Biol Chem |
| Year | 2002 |
| Volume | 277 |
| Pages | 17548-55 |
| Authors | Reckenfelderbaumer N, Krauth-Siegel RL |
| Title |
Catalytic properties, |
| Related PDB | |
| Related UniProtKB | |
| [27] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 12111385 |
| Journal | J Mol Model (Online) |
| Year | 2002 |
| Volume | 8 |
| Pages | 173-83 |
| Authors | Iribarne F, Paulino M, Aguilera S, Murphy M, Tapia O |
| Title | Docking and molecular dynamics studies at trypanothione reductase and glutathione reductase active sites. |
| Related PDB | |
| Related UniProtKB | |
| [28] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 15102853 |
| Journal | J Biol Chem |
| Year | 2004 |
| Volume | 279 |
| Pages | 29493-500 |
| Authors | Saravanamuthu A, Vickers TJ, Bond CS, Peterson MR, Hunter WN, Fairlamb AH |
| Title | Two interacting binding sites for quinacrine derivatives in the active site of trypanothione reductase: a template for drug design. |
| Related PDB | 1gxf |
| Related UniProtKB | |
| Comments |
|---|
|
As in its homologous enzymes (thioredoxin reductase; D00045 & dihydrolipoyl dehydrogenase; T00017 in EzCatDB), (A) Hydride or electron transfer from NADPH to FAD (Reduction of FAD by NADPH) (part of reductive half-reaction) (B) Electron transfer from reduced FAD (FADH2) to active-site disulfide (Cys-Cys) (part of reductive half-reaction) (C) Electron transfer from active site cysteine residues to trypanothione disulfide substrate (Reduction of substrate [trypanothione disulfide] at the active site) |
| Created | Updated |
|---|---|
| 2004-12-24 | 2009-02-26 |