Information on EC 1.8.1.10 - CoA-glutathione reductase

395012, 395105, 395107

Substrates: -
Products: -

CoA-glutathione + NADPH

glutathione + CoA + NADP+

Substrates: -
Products: -

CoA-glutathione + NADPH

glutathione + CoA + NADP+

Substrates: high substrate specificity
Products: -

CoA-glutathione + NADPH

glutathione + CoA + NADP+

Substrates: may be important in metabolism of CoASSG
Products: -

CoA-glutathione + NADPH

glutathione + CoA + NADP+

Substrates: -
Products: -

additional information

Substrates: no reduction of disulfides such as cystine, cystamine, panthetine, and insulin
Products: -

additional information

Substrates: no reduction of CoASSCys, GSSCys or CysSSCys
Products: -

show all columns Go to Natural Substrate Search

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NATURAL SUBSTRATE

NATURAL PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

LITERATURE

COMMENTARY

REVERSIBILITY
r=reversible
ir=irreversible
?=not specified

CoA disulfide + NADPH

CoA + NADP+

CoA-glutathione + NADPH

glutathione + CoA + NADP+

3 entries

CoA disulfide + NADPH

CoA + NADP+

Substrates: central role in thiol metabolism
Products: -

CoA disulfide + NADPH

CoA + NADP+

Substrates: central role in thiol metabolism
Products: -

CoA-glutathione + NADPH

glutathione + CoA + NADP+

Escherichia coli

395106

CoA-glutathione + NADPH

glutathione + CoA + NADP+

Substrates: -
Products: -

CoA-glutathione + NADPH

glutathione + CoA + NADP+

Substrates: may be important in metabolism of CoASSG
Products: -

show all columns Go to Cofactor Search

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COFACTOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

FAD

flavoprotein, gene with two FAD-binding regions

NADPH

NADPH

NADPH

NADPH-dependent

NADPH

NADPH-dependent

NADPH

NADPH-dependent

395012, 395107, 395108

NADPH

NADPH-dependent

NADPH

gene with one NADPH-binding region

show all columns Go to Inhibitor Search

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INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

phosphate

25 mM, partially inhibits

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KM VALUE [mM]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.014

CoA disulfide

recombinant enzyme expressed in E. coli

0.2 - 0.23

CoA-glutathione

0.0019

NADPH

recombinant enzyme expressed in E. coli

0.2

CoA-glutathione

at pH 5.5 and a fixed value of 110 nmol NADPH

0.23

CoA-glutathione

at pH 5.75 and a fixed value of 110 nmol NADPH

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TURNOVER NUMBER [1/s]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

1100

CoA disulfide

show all columns Go to Specific Activity Search

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SPECIFIC ACTIVITY [µmol/min/mg]

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

0.0007

alloxan diabetic rats, liver extract

0.00085

normal rats, liver extract

additional information

4 entries

additional information

Escherichia coli

specific activity of enzyme in crude extract increases during growth from early log phase into stationary phase and during a shift from aerobic to anaerobic growth

395106

additional information

additional information

additional information

show all columns Go to pH Optimum Search

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pH OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

5.5

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5.8

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TEMPERATURE OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

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assay at

assay at

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks include all textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks + FRENDAco-occurrence of enzyme names and organism names (less precise)

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ORGANISM

COMMENTARY

LITERATURE

UNIPROT

SEQUENCE DB

SOURCE

brenda

strain ATCC 1946

brenda

strain 8325-4

brenda

strain 8325-4

brenda

brenda

male albino, normal and alloxan diabetic rats, no change of enzyme activity and CoASSG content in diabetic rats

brenda

male sprague-dawley rats

brenda

show all columns Go to Source Tissue Search

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks

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SOURCE TISSUE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

SOURCE

brenda

brenda

brenda

brenda

brenda

395012, 395105, 395107, 395108

brenda

brenda

brenda

brenda

brenda

show all columns Go to Localization Search

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks

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LOCALIZATION

ORGANISM

UNIPROT

COMMENTARY

GeneOntology No.

LITERATURE

SOURCE

brenda

Highest Expressing Human Cell Lines

Filter by:

Cell Line Links

Gene Links

Go to AA Sequence and Transmembrane Helices SearchGo to Localization Prediction

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UNIPROT

ENTRY NAME

ORGANISM

NO. OF AA

NO. OF TRANSM. HELICES

MOLECULAR WEIGHT[Da]

SOURCE

SEQUENCE

LOCALIZATION PREDICTION

The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).

A0A6B9VM58 pBLAST

A0A6B9VM58_STEFE

Steinernema feltiae

8082

TrEMBL

Show Sequence

other Location (Reliability: 2)

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MOLECULAR WEIGHT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

108000

sucrose density gradient ultracentrifugation

42500

gel filtration, one protein with CoASSG reductase and GSSG reductase activities, EC 1.6.4.2

49200

2 * 49200, calculated from the nucleotide sequence

90000

native molecular weight

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SUBUNIT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

dimer

dimer

2 * 49200, calculated from the nucleotide sequence

dimer

2 * 49200, calculated from the nucleotide sequence

Go to Storage Stability Search

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STORAGE STABILITY

ORGANISM

UNIPROT

LITERATURE

4°C, dialyzed extract, 16 hours, stable

Go to Purification (commentary) Search

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PURIFICATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

143fold partial purification, separated from GSSG reductase activity, EC 1.6.4.2

289fold purification

not separated from GSSG reductase activity, EC 1.6.4.2

395107, 395108

purification of recombinant CoADR, expressed in Escherichia coli

Go to Cloned (commentary) Search

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CLONED (Commentary)

ORGANISM

UNIPROT

LITERATURE

cdr gene encoding coenzyme A glutathione disulfide reductase is cloned, sequenced and overexpressed in Escherichia coli BL21 using the pET expression system, gene encodes a 438-amino acid polypeptide

show all columns Go to Application Search

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APPLICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

medicine

pharmacology

medicine

potential point of intervention in the treatment of staphylococcal infections

medicine

potential point of intervention in the treatment of staphylococcal infections

pharmacology

anti-staphylococcal agent, possible target for the design of selective inhibitors that would interrupt the thiol metabolism of the human pathogen Staphylococcus aureus

pharmacology

top print hide References Search

anti-staphylococcal agent, possible target for the design of selective inhibitors that would interrupt the thiol metabolism of the human pathogen Staphylococcus aureus

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REF.

AUTHORS

TITLE

JOURNAL

VOL.

PAGES

YEAR

ORGANISM (UNIPROT)

PUBMED ID

SOURCE

Dyar, R.E.; Wilken, D.R.

Rat liver levels of coenzyme A-glutathione and of enzymes in its metabolism

Arch. Biochem. Biophys.

153

619-626

1972

Rattus norvegicus

4662104

brenda

395105

Acuna, R.; Vargas, E.; Ondarza, R.N.

Distribution of GSSG- and CoASSG-reductase in rat tissues

Temas Bioquim. Actual. (Pina, E. , Pena, A. , Chagoya de Sanchez, V. , eds. )

355-359

1978

Rattus norvegicus

brenda

395106

Loewen, P.C.

Identification of a coenzyme A--glutathione disulfide (DSI), a modified coenzyme A disulfide (DSII), and a NADPH-dependent coenzyme A--glutathione disulfide reductase in E. coli

Can. J. Biochem.

1019-1027

1977

Escherichia coli

334350

brenda

Eriksson, S.; Guthenberg, C.; Mannervik, B.

The nature of the enzymatic reduction of the mixed disulfide of coenzyme A and glutathione

FEBS Lett.

296-300

1974

Rattus norvegicus

4605303

brenda

Ondarza, R.N.; Escamilla, E.; Gutierrez, J.; de la Chica, G.

CoAS-Sglutathione and GSSG reductases from rat liver. Two disulfide oxidoreductase activities in one protein entity

Biochim. Biophys. Acta

341

162-171

1974

Rattus norvegicus

4151341

brenda

Ondarza, R.N.; Abney, R.; Lopez-Colome, A.M.

Characterization of a NADPH-dependent coenzyme A-SS-glutathione reductase from yeast

Biochim. Biophys. Acta

191

239-248

1969

Saccharomyces cerevisiae

4390951

brenda