1.8.98.2: sulfiredoxin

This is an abbreviated version!
For detailed information about sulfiredoxin, go to the full flat file.

Word Map on EC 1.8.98.2

1.8.98.2

peroxiredoxins

hyperoxidation

thioredoxins

overoxidized

sulfenic

peroxidatic

txnrd1

sulfinylated

deglutathionylation

prxiii

prdxs

cys-so2h

medicine

drug development

Reaction

+ 2 R-SH =

Synonyms

AtSrx, cysteine-sulfinic acid reductase, neoplastic progression 3, peroxiredoxin-(S-hydroxy-S-oxocysteine) reductase, protein cysteine sulfinic acid reductase, Srx, Srx1, Srxn1, sulfiredoxin, sulfiredoxin 1, sulfiredoxin-1, sulphiredoxin

ECTree

1 Oxidoreductases

1.8 Acting on a sulfur group of donors

1.8.98 With other, known, physiological acceptors

1.8.98.2 sulfiredoxin

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Results	in table
1	Activating Compound
1793	AA Sequence
5	Application
1	CAS Registry Number
19	Cloned(Commentary)
17	Cofactor
4	Crystallization (Commentary)
228	Disease/ Diagnostics
8	Expression
18	General Information
2	IC50 Value
9	Inhibitors
8	KM Value [mM]
20	Localization
11	Metals/Ions
6	Molecular Weight [Da]
21	Natural Substrates/ Products (Substrates)
50	Organism
26	PDB ID
3	pH Optimum
3	pI Value
36	Protein Variants
9	Purification (Commentary)
1	Reaction
17	Reaction Type
44	Reference
40	Source Tissue
73	Substrates and Products (Substrate)
3	Subunits
54	Synonyms
1	Systematic Name
4	Temperature Optimum [°C]
5	Turnover Number [1/s]

Inhibitors

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Inhibitors on EC 1.8.98.2 - sulfiredoxin

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1,9-pyrazoloanthrone

Rattus norvegicus

742457

4-(((4-(4-(2-chlorophenyl)piperazin-1-yl)-6-(2,4-dihydroxy-5-isopropylphenyl)pyrimidin-2-yl)thio)methyl)benzoic acid

Homo sapiens

Q9BYN0

LMT-328, synthesis, a derivative of Jl4, more potent inhibitor than J14. The simulation, LMT-328 shows fast stabilization and tight binding with Srx. LMT-328 has a similar binding pose as the lead compound, J14, overview

765246

4-[[[4-[4-(2-chlorophenyl)-1-piperazinyl]-6-phenyl-2-pyrimidinyl]thio]methyl]-benzoic acid

Homo sapiens

Q9BYN0

J14, synthesis, interferes with the antioxidant activity of Srx at the molecular level. Identification of two possible inhibition mechanisms of Srx by J14. Using molecular dynamics simulations and binding free energy calculations, it is confirmed that J14 binds to the ATP binding site, J14 acts as a competitive inhibitor of ATP. J14 can serve as a protein-protein interaction inhibitor that interferes with the binding between Prx and Srx

N-acetylcysteine

RNAi

siRNA

additional information

2 entries