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
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1.13.11.49
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perchlorate
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chlorate
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dechloromonas
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perchlorate-reducing
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dismutases
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clo2
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dismutation
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high-spin
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low-spin
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dechloratans
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defluvii
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chlorate-reducing
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nitrospira
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ideonella
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aromatica
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azospira
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hemqs
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environmental protection
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molecular biology
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biotechnology
- 1.13.11.49
- perchlorate
- chlorate
- dechloromonas
-
perchlorate-reducing
- dismutases
- clo2
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dismutation
-
high-spin
-
low-spin
- dechloratans
- defluvii
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chlorate-reducing
- nitrospira
- ideonella
- aromatica
- azospira
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hemqs
- environmental protection
- molecular biology
- biotechnology
Reaction
Synonyms
chlorite dismutase, CLD, Cyan7425_1434, dimutase, chlorite, HemQ, Pfam chlorite dismutase, PitA
ECTree
1.13.11.49 chlorite O2-lyaseAdvanced search results
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results (Subunits
Subunits on EC 1.13.11.49 - chlorite O2-lyase
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SUBUNIT 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dimer
conformational and thermal stability of recombinant dimeric Cld from Nitrobacter winogradskyi, overview
hexamer
homodimer
homopentamer
homopentamer or homohexamer
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5 or 6 * 30300, calculated from amino acid sequence
homotetramer
monomer
pentamer
tetramer
additional information
hexamer
6 * 30000, multiple anomalous dispersion crystal structure, one heme per monomer (histidine 170 axial heme ligand), arginine 183 probably with essential role in substrate positioning and activation, activity of the hexamer not measurable because of the presence of the thiocyanate inhibitor, each monomer appears to be acting on its own, therefore, different quaternary states may be biologically relevant depending on protein concentration, pH, or other factors
hexamer
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6 * 30000, multiple anomalous dispersion crystal structure, one heme per monomer (histidine 170 axial heme ligand), arginine 183 probably with essential role in substrate positioning and activation, activity of the hexamer not measurable because of the presence of the thiocyanate inhibitor, each monomer appears to be acting on its own, therefore, different quaternary states may be biologically relevant depending on protein concentration, pH, or other factors
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homodimer
subunit interface and active site structures, structure modeling, overview
homopentamer
each monomer of NdCld is characterized by two topologically equivalent four-stranded antiparallel beta-sheets forming a beta-barrel, flanked on both sides by six alpha-helices, overview
homotetramer
Stutzerimonas chloritidismutans
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4 * 31000, heme content 1.5 mol Fe2+/mol enzyme (calculated from Soret peak shift measurement), 2.2 mol Fe2+/mol enzyme (metal analysis by ICP-MS)
homotetramer
Stutzerimonas chloritidismutans AW-1 / DSM 13592
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4 * 31000, heme content 1.5 mol Fe2+/mol enzyme (calculated from Soret peak shift measurement), 2.2 mol Fe2+/mol enzyme (metal analysis by ICP-MS)
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pentamer
5 * 30000 Da, tandem mass spectrometry, native mass spectrometry, active state in solution
pentamer
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5 * 30000 Da, tandem mass spectrometry, native mass spectrometry, active state in solution
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pentamer
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conformational and thermal stability of recombinant pentameric Cld from Nitrospira defluvii, overview
tetramer
4 * 30000 Da, elution position on a gel-filtration column using Stokes radius to determine molecular weight points to globular tetramer, collisional activation of the ions ejects one monomer of the pentamer, so that low-charged tetramer counter complex ions are also observed with native mass spectrometry
tetramer
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4 * 30000 Da, elution position on a gel-filtration column using Stokes radius to determine molecular weight points to globular tetramer, collisional activation of the ions ejects one monomer of the pentamer, so that low-charged tetramer counter complex ions are also observed with native mass spectrometry
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additional information
the Cld-like protein from the chemolithoautotrophic nitrite oxidizer Nitrobacter winogradskyi is significantly smaller than all previously known chlorite dismutases
additional information
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the Cld-like protein from the chemolithoautotrophic nitrite oxidizer Nitrobacter winogradskyi is significantly smaller than all previously known chlorite dismutases
