1.13.11.49: chlorite O2-lyase
This is an abbreviated version!
For detailed information about chlorite O2-lyase, go to the full flat file.
Word Map on EC 1.13.11.49
-
1.13.11.49
-
perchlorate
-
chlorate
-
dechloromonas
-
perchlorate-reducing
-
dismutases
-
clo2
-
dismutation
-
high-spin
-
low-spin
-
dechloratans
-
defluvii
-
chlorate-reducing
-
nitrospira
-
ideonella
-
aromatica
-
azospira
-
hemqs
-
environmental protection
-
molecular biology
-
biotechnology
- 1.13.11.49
- perchlorate
- chlorate
- dechloromonas
-
perchlorate-reducing
- dismutases
- clo2
-
dismutation
-
high-spin
-
low-spin
- dechloratans
- defluvii
-
chlorate-reducing
- nitrospira
- ideonella
- aromatica
- azospira
-
hemqs
- environmental protection
- molecular biology
- biotechnology
Reaction
Synonyms
chlorite dismutase, CLD, Cyan7425_1434, dimutase, chlorite, HemQ, Pfam chlorite dismutase, PitA
ECTree
Advanced search results
Cofactor
Cofactor on EC 1.13.11.49 - chlorite O2-lyase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
heme
-
HemQ's equilibrium affinity for heme is in the low micromolar range. Holo-HemQ reconstituted with heme exhibits heme lysis after less than 50 turnovers with peroxide and less than 10 turnovers with chlorite. The heme-free apoprotein aggregates or unfolds over time. HemQ uses heme or porphyrin-like organic molecules as substrates. Heme in HemQ degrades in the presence of relatively small numbers of equivalents of H2O2, chlorite, or peracetic acid
heme
-
at pH 6.0, ferric Cld exhibits a Soret band maximum at 405 nm, a broad alpha/beta band envelope at 505 nm with a small shoulder at 540 nm, and a charge transfer band at 645 nm
heme
resting ferric high-spin axially symmetric heme enzyme, standard reduction potential of the Fe(III)/Fe(II) couple of -126 mV at pH 7.0
heme
wild-type Cld shows a variety of low- and high-spin ferric heme forms. Addition of an axial ligand, such as azide or imidazole, removes this heterogeneity almost entirely