1.12.1.2: hydrogen dehydrogenase
This is an abbreviated version!
For detailed information about hydrogen dehydrogenase, go to the full flat file.
Word Map on EC 1.12.1.2
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1.12.1.2
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alcaligenes
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eutrophus
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hydrogenases
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ralstonia
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hydrogen-oxidizing
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h2-dependent
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lithoautotrophic
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thiocapsa
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roseopersicina
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h2-oxidizing
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oxygen-tolerant
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synthesis
- 1.12.1.2
- alcaligenes
- eutrophus
- hydrogenases
-
ralstonia
-
hydrogen-oxidizing
-
h2-dependent
-
lithoautotrophic
-
thiocapsa
- roseopersicina
-
h2-oxidizing
-
oxygen-tolerant
- synthesis
Reaction
Synonyms
bidirectional hydrogenase, bidirectional Ni-Fe hydrogenase, bidirectional NiFe-hydrogenase, bidirectional [NiFe] hydrogenase, dehydrogenase, hydrogen, FeHyd, H2:NAD+ oxidoreductase, H2ase, Hox, Hox hydrogenase, Hox type hydrogenase, HoxE, HoxEFUYH, HoxF, HoxFUYHI2, HoxH, HoxS, HoxU, HoxY, hydrogen-evolving enzyme, hydrogenase, Hyn, iron-hydrogenase, NAD+-reducing hydrogenase, NAD+-reducing NiFe hydrogenase, NAD+-reducing [NiFe]-hydrogenase, NAD-dependent hydrogenase, NAD-reducing hydrogenase, NADH-dependent Fe-only hydrogenase, NiFe hydrogenase, NiFe-type reversible hydrogenase, SH, soluble hydrogenase, soluble [NiFe]-hydrogenase, [FeFe] hydrogenase, [FeFe]-hydrogenase, [NiFe] H2ase, [NiFe] hydrogenase, [NiFe]-hydrogenase
ECTree
1.12.1.2 hydrogen dehydrogenaseAdvanced search results
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results (Inhibitors
Inhibitors on EC 1.12.1.2 - hydrogen dehydrogenase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
diethyl dicarbonate
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chemical modification of active site His residues results in reduced enzymatic hydrogenase and diaphorase activities, pH-dependence and kinetics of modifications/inactivation
DTNB
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modification of thiol groups of activated enzyme results in rapid inactivation of both activities, modification of the residues of nonactivated enzyme has small effects on the enzyme activities, pH-dependence and kinetics of modifications/inactivation
iodoacetic acid
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modification of thiol groups of activated enzyme results in rapid inactivation of both activities, modification of the residues of nonactivated enzyme has small effects on the enzyme activities, pH-dependence and kinetics of modifications/inactivation
Ni2+
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0.5-1 mM, strong inhibition of artificial electron acceptor reduction
O2
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irreversible enzyme inhibition by oxygen occurs if the CN- bound to Ni2+ is irreversibly removed or if the enzyme is reduced by NADH
O2
incubation of subunits HoxHY with O2 at high potentials causes slow inactivation, but activity is recovered within seconds at potentials below -170 mV at 30°C, even in the presence of 2% O2; incubation of subunits HoxHY with O2 at high potentials causes slow inactivation, but activity is recovered within seconds at potentials below -170 mV at 30°C, even in the presence of 2% O2
p-chloromercuribenzoate
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0.02 mM, complete inhibition, reversed by addition of glutathione
additional information
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release of one FMN reduces the NAD+ reduction by 90%, but is reversible by addition of excess FMN, insensitivity towards oxygen, with all 4 CN- groups bound to the enzyme, and towards CO
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additional information
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when light adapted cells are transferred to darkness the expression of hoxE and hoxF is only slightly affected, while the transcript levels of hoxU, hoxY and hoxH are significantly (3-5fold) decreased. Putative regulators of hox gene expression sll0359 is suppressed in dark to a similar extent as hoxU, hoxY and hoxH. The transcriptional regulator lexA shows the opposite expression pattern than that of the hox genes, since it decreases in the light. When cells in microaerobic conditions are transferred to darkness the transcript levels of hoxU, hoxY, hoxH transcripts slightly decrease
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