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PDOC00395
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1995-07-26
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***********************
* Catalase signatures *
***********************
Catalase (EC 1.11.1.6) [1,2,3] is an enzyme, present in all aerobic cells,
that decomposes hydrogen peroxide to molecular oxygen and water. Its main
function is to protect cells from the toxic effects of hydrogen peroxide. In
eukaryotic organisms and in some prokaryotes catalase is a molecule composed
of four identical subunits. Each of the subunits binds one protoheme IX group.
A conserved tyrosine serves as the heme proximal side ligand. We have used the
region around this residue as a first signature pattern; it also includes a
conserved arginine that participates in heme-binding. A conserved histidine
has been shown to be important for the catalytic mechanism of the enzyme. We
have used the region around this residue as a second signature pattern.
-Consensus pattern: R-[LIVMFA]-F-[GAST]-Y-x-D-[AST]-[QEH]
[Y is the proximal heme-binding ligand]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in SWISS-PROT: NONE.
-Consensus pattern: F-x-[RH]-x(4)-[EQ]-R-x(2)-H-x(2)-[GAS](3)
[H is an active site residue]
-Sequences known to belong to this class detected by the pattern: ALL, except
for Bacillus firmus catalase.
-Other sequence(s) detected in SWISS-PROT: NONE.
-Note: some prokaryotic catalases belong to the peroxidase family (see the
relevant section).
-Last update: October 1993 / Patterns and text revised.
[ 1] Murthy M.R.N., Reid T.J. III, Sicignano A., Tanaka N., Rossmann M.G.
J. Mol. Biol. 152:465-499(1981).
[ 2] Melik-Adamyan W.R., Barynin V.V., Vagin A.A., Borisov V.V.,
Vainshtein B.K., Fita I., Murthy M.R.N., Rossmann M.G.
J. Mol. Biol. 188:63-72(1986).
[ 3] von Ossowki I., Hausner G. Loewen P.C.
J. Mol. Evol. 37:71-76(1993).