Trypanothione reductase

Details

Name
Trypanothione reductase
Synonyms
  • 1.8.1.12
  • N(1),N(8)-bis(glutathionyl)spermidine reductase
  • TR
Gene Name
TPR
Organism
Trypanosoma cruzi
Amino acid sequence
>lcl|BSEQ0011099|Trypanothione reductase
MMSKIFDLVVIGAGSGGLEAAWNAATLYKKRVAVIDVQMVHGPPFFSALGGTCVNVGCVP
KKLMVTGAQYMEHLRESAGFGWEFDRTTLRAEWKKLIAVKDEAVLNINKSYEEMFRDTEG
LEFFLGWGSLESKNVVNVRESADPASAVKERLETENILLASGSWPHMPNIPGIEHCISSN
EAFYLPEPPRRVLTVGGGFISVEFAGIFNAYKPKDGQVTLCYRGEMILRGFDHTLREELT
KQLTANGIQILTKENPAKVELNADGSKSVTFESGKKMDFDLVMMAIGRSPRTKDLQLQNA
GVMIKNGGVQVDEYSRTNVSNIYAIGDVTNRVMLTPVAINEAAALVDTVFGTNPRKTDHT
RVASAVFSIPPIGTCGLIEEVASKRYEVVAVYLSSFTPLMHNISGSKYKTFVAKIITNHS
DGTVLGVHLLGDNAPEIIQGVGICLKLNAKISDFYNTIGVHPTSAEELCSMRTPSYYYVK
GEKMEKPSEASL
Number of residues
492
Molecular Weight
53867.475
Theoretical pI
6.68
GO Classification
Functions
disulfide oxidoreductase activity / flavin adenine dinucleotide binding / trypanothione-disulfide reductase activity
Processes
cell redox homeostasis
Components
cytoplasm
General Function
Trypanothione-disulfide reductase activity
Specific Function
Trypanothione is the parasite analog of glutathione; this enzyme is the equivalent of glutathione reductase.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0003079|1479 bp
ATGATGTCAAAAATTTTTGATTTGGTTGTCATTGGCGCCGGCTCGGGCGGACTGGAGGCT
GCTTGGAACGCGGCGACACTCTACAAGAAGCGGGTTGCGGTGATTGATGTTCAGATGGTT
CACGGGCCCCCGTTTTTTTCTGCTCTAGGCGGCACGTGTGTCAATGTTGGCTGCGTTCCG
AAGAAATTGATGGTTACAGGGGCCCAATACATGGAACACCTGCGCGAGTCCGCTGGGTTC
GGGTGGGAGTTTGATCGCACCACTCTCAGGGCGGAATGGAAGAAACTTATTGCTGTCAAG
GACGAGGCGGTGCTGAATATCAACAAGAGTTATGAGGAGATGTTTCGGGACACGGAGGGT
CTGGAGTTTTTTCTGGGCTGGGGATCACTGGAGTCAAAGAATGTCGTCAATGTTCGCGAG
AGTGCCGACCCGGCCAGCGCAGTGAAGGAGCGCCTGGAGACGGAGAACATTCTACTTGCC
AGTGGTTCGTGGCCGCACATGCCAAACATCCCTGGTATTGAGCATTGCATCAGCAGCAAT
GAGGCATTTTACCTGCCGGAGCCACCGCGTCGTGTCCTCACTGTCGGCGGAGGTTTCATT
TCCGTGGAGTTCGCCGGCATTTTTAACGCCTACAAGCCGAAAGACGGACAAGTGACGTTG
TGCTACCGCGGTGAAATGATCCTTCGTGGCTTTGACCACACTCTCCGTGAGGAACTCACA
AAGCAGCTCACCGCCAACGGCATTCAAATCCTTACAAAGGAAAATCCGGCCAAGGTGGAG
TTGAACGCGGATGGCAGCAAAAGTGTTACTTTCGAGAGCGGCAAAAAGATGGACTTTGAT
CTTGTCATGATGGCGATTGGCCGTTCTCCCCGAACAAAGGATTTACAGCTGCAAAACGCC
GGCGTCATGATCAAGAACGGTGGTGTGCAGGTGGACGAGTACTCGCGCACGAATGTTTCC
AACATTTACGCCATCGGTGACGTCACAAATCGTGTCATGTTGACACCCGTTGCCATAAAT
GAAGCCGCTGCCCTTGTGGATACCGTCTTTGGTACCAATCCGCGAAAGACGGACCACACC
CGTGTGGCGAGTGCCGTCTTCTCTATTCCTCCAATTGGTACCTGCGGTCTCATTGAAGAG
GTTGCATCCAAGCGCTACGAGGTGGTGGCGGTATACCTTTCCAGCTTTACCCCGCTCATG
CACAACATCAGCGGATCAAAGTATAAGACTTTTGTTGCAAAGATAATTACCAACCACTCC
GATGGCACTGTGCTTGGTGTACATCTTCTTGGGGACAATGCCCCAGAAATCATCCAAGGT
GTTGGTATCTGTCTCAAGTTAAATGCCAAAATATCCGACTTCTACAACACTATTGGTGTG
CATCCCACAAGTGCGGAGGAGCTGTGCTCCATGCGCACTCCTTCTTACTACTATGTTAAA
GGTGAGAAGATGGAAAAGCCTTCAGAGGCATCTCTGTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP28593
UniProtKB Entry NameTYTR_TRYCR
GenBank Protein ID162317
GenBank Gene IDM38051
General References
  1. Sullivan FX, Walsh CT: Cloning, sequencing, overproduction and purification of trypanothione reductase from Trypanosoma cruzi. Mol Biochem Parasitol. 1991 Jan;44(1):145-7. [PubMed:2011150]
  2. Borges A, Cunningham ML, Tovar J, Fairlamb AH: Site-directed mutagenesis of the redox-active cysteines of Trypanosoma cruzi trypanothione reductase. Eur J Biochem. 1995 Mar 15;228(3):745-52. [PubMed:7737173]
  3. Krauth-Siegel RL, Sticherling C, Jost I, Walsh CT, Pai EF, Kabsch W, Lantwin CB: Crystallization and preliminary crystallographic analysis of trypanothione reductase from Trypanosoma cruzi, the causative agent of Chagas' disease. FEBS Lett. 1993 Feb 8;317(1-2):105-8. [PubMed:8428618]
  4. Lantwin CB, Schlichting I, Kabsch W, Pai EF, Krauth-Siegel RL: The structure of Trypanosoma cruzi trypanothione reductase in the oxidized and NADPH reduced state. Proteins. 1994 Feb;18(2):161-73. [PubMed:8159665]
  5. Zhang Y, Bond CS, Bailey S, Cunningham ML, Fairlamb AH, Hunter WN: The crystal structure of trypanothione reductase from the human pathogen Trypanosoma cruzi at 2.3 A resolution. Protein Sci. 1996 Jan;5(1):52-61. [PubMed:8771196]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB02240Quinacrine mustardexperimentalunknowninhibitorDetails
DB03147Flavin adenine dinucleotideapprovedunknownDetails
DB03470TrypanothioneexperimentalunknownDetails
DB04299Maleic AcidexperimentalunknownDetails