The molecular peculiarities of catalase-peroxidases.

Abstract:

:In developing ideas of how protein structure modifies haem reactivity, the activity of Class I of the plant peroxidase superfamily (including cytochrome c peroxidase, ascorbate peroxidase and catalase-peroxidases (KatGs)) is an exciting field of research. Despite striking sequence homologies, there are dramatic differences in catalytic activity and substrate specificity with KatGs being the only member with substantial catalase activity. Based on multiple sequence alignment performed for Class I peroxidases, we present a hypothesis for the pronounced catalase activity of KatGs. In their catalytic domains KatGs are shown to possess three large insertions, two of them are typical for KatGs showing highly conserved sequence patterns. Besides an extra C-terminal copy of the ancestral hydroperoxidase gene resulting from gene duplication, these two large loops are likely to control the orientation of both the haem group and of essential residues in the active site. They seem to modulate the access of substrates to the prosthetic group at the distal side as well as the flexibility and character of the bond between the proximal histidine and the ferric iron. The hypothesis presented opens new possibilities in the rational engineering of peroxidases.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Zámocký M,Regelsberger G,Jakopitsch C,Obinger C

doi

10.1016/s0014-5793(01)02237-2

keywords:

subject

Has Abstract

pub_date

2001-03-16 00:00:00

pages

177-82

issue

3

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(01)02237-2

journal_volume

492

pub_type

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