1.21.4.2: glycine reductase
This is an abbreviated version!
For detailed information about glycine reductase, go to the full flat file.
Word Map on EC 1.21.4.2
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1.21.4.2
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selenocysteine
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clostridial
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sticklandii
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eubacterium
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acidaminophilum
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selenium-dependent
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purinolyticum
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selenocysteine-containing
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d-proline
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opal
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selenols
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selenoenzymes
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selenoether
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sporogenes
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selenium-containing
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cylindrosporum
- 1.21.4.2
- selenocysteine
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clostridial
- sticklandii
- eubacterium
- acidaminophilum
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selenium-dependent
- purinolyticum
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selenocysteine-containing
- d-proline
-
opal
-
selenols
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selenoenzymes
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selenoether
- sporogenes
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selenium-containing
- cylindrosporum
Reaction
Synonyms
glycine reductase, GrdA
ECTree
1.21.4.2 glycine reductaseAdvanced search results
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results (Inhibitors
Inhibitors on EC 1.21.4.2 - glycine reductase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
acetyl phosphate
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inhibits protein C activity, although a substrate
Bromoacetate
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75Se-labeled protein A preparation is inactivated at pH 6, 25°C, for 10 min in presence of 10 mM bromoacetate by about 25%
KCl
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the ability of protein component C to catalyse the arsenate-dependent decomposition of acetyl phosphate is inhibited
(NH4)2SO4
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inhibits the ability of protein component C to catalyse the arsenate-dependent decomposition of acetyl phosphate
(NH4)2SO4
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70% loss of activity at 300 mM; inhibits the ability of protein component C to catalyse the arsenate-dependent decomposition of acetyl phosphate
iodoacetate
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the ability of protein component C to catalyse the arsenate-dependent decomposition of acetyl phosphate is inhibited, but protein C is protected from inactivation by treatment acetyl phosphate
iodoacetate
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the ability of protein component C to catalyse the arsenate-dependent decomposition of acetyl phosphate is inhibited, but protein C is protected from inactivation by treatment acetyl phosphate
additional information
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inactivation of selenoprotein A from Clostridium purinolyticum by sheep antibodies elicited to selenoprotein A from Clostridium stricklandii
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additional information
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inactivation of selenoprotein A from Clostridium purinolyticum by sheep antibodies elicited to selenoprotein A from Clostridium stricklandii
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additional information
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antibodies raised against the thioredoxin reductase-like flavoprotein or thioredoxin inhibit to a high extent
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