KEGG ENZYME: 1.8.1.12

ENZYME: 1.8.1.12

Entry

EC 1.8.1.12                 Enzyme

Name

trypanothione-disulfide reductase;
trypanothione reductase;
NADPH2:trypanothione oxidoreductase

Class

Oxidoreductases;
Acting on a sulfur group of donors;
With NAD+ or NADP+ as acceptor

Sysname

trypanothione:NADP+ oxidoreductase

Reaction(IUBMB)

trypanothione + NADP+ = trypanothione disulfide + NADPH + H+ [RN:R03821]

Reaction(KEGG)

R03821;
(other) R08356 R08357

Substrate

trypanothione [CPD:C02090];
NADP+ [CPD:C00006]

Product

trypanothione disulfide [CPD:C03170];
NADPH [CPD:C00005];
H+ [CPD:C00080]

Comment

Trypanothione disulfide is the oxidized form of N1,N8-bis(glutathionyl)-spermidine from the insect-parasitic trypanosomatid Crithidia fasciculata. The enzyme from Crithidia fasciculata is a flavoprotein (FAD), whose activity is dependent on a redox-active cystine at the active centre. (cf. EC 1.8.1.7, glutathione-disulfide reductase)

History

EC 1.8.1.12 created 1989 as EC 1.6.4.8, transferred 2002 to EC 1.8.1.12

Pathway

ec00480

Glutathione metabolism

ec01100

Metabolic pathways

Orthology

K04283

trypanothione-disulfide reductase

Genes

TBR:	Tb10.406.0520

TBG:	TbgDal_X12680

TCR:

503555.30

LMA:	LMJF_05_0350(TRYR)

LIF:	LINJ_05_0350(TRYR)

LDO:	LDBPK_050350

LMI:	LMXM_05_0350

LMAT:

92517582(LSCM1_07710)

LBZ:	LBRM_05_0350(TRYR)

LPAN:

LPMP_050340(TRYR)

LOI:	92363849(LSCM4_08039)

LEIS:

94183168(GH5_07947)

LENR:

94174763(CUR178_07612)

LEIN:

94191590(JIQ42_08021)

PHET:

94293377(JKF63_07361)

» show all

Reference

1 [PMID:3718941]

Authors

Shames SL, Fairlamb AH, Cerami A, Walsh CT

Title

Purification and characterization of trypanothione reductase from Crithidia fasciculata, a newly discovered member of the family of disulfide-containing flavoprotein reductases.

Journal

Biochemistry 25:3519-26 (1986)
DOI:10.1021/bi00360a007

Sequence

[ag:CAA78264]

Reference

2 [PMID:9057833]

Authors

Marsh IR, Bradley M.

Title

Substrate specificity of trypanothione reductase.

Journal

Eur J Biochem 243:690-4 (1997)
DOI:10.1111/j.1432-1033.1997.00690.x