Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

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

Reaction

peroxiredoxin-(S-hydroxy-S-oxocysteine)
+
ATP
+ 2 R-SH =
peroxiredoxin-(S-hydroxycysteine)
+
ADP
+
phosphate
+
R-S-S-R

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

General Information

General Information on EC 1.8.98.2 - sulfiredoxin

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
AtSrx has more positive charges than human enzyme HsSrx. The theoretical pI of AtSrx is 9.86, much higher than 5.47 of HsSrx. There are 10 arginine residues and 7 lysine residues in AtSrx but only 5 arginine residues and 3 lysine residues in HsSrx. For negatively charged amino acids residues, there are 6 glutamic acid residues and 4 aspartic acid residues in AtSrx, while there are 2 glutamic acid residues and 8 aspartic acid residues in HsSrx. Abundant charged amino acids of AtSrx provide more positive charge at ADP binding pocket and more interaction with active
malfunction
physiological function
additional information