4.2.1.104: cyanase
This is an abbreviated version!
For detailed information about cyanase, go to the full flat file.
Word Map on EC 4.2.1.104
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4.2.1.104
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bicarbonate
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bicarbonate-dependent
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anderson
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fuchs
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pseudoalcaligenes
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molecular biology
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nitrospira
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decameric
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environmental protection
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biotechnology
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drug development
- 4.2.1.104
- bicarbonate
-
bicarbonate-dependent
-
anderson
-
fuchs
- pseudoalcaligenes
- molecular biology
- nitrospira
-
decameric
- environmental protection
- biotechnology
- drug development
Reaction
Synonyms
107368746, AtCYN, cyanase, cyanate aminohydrolase, cyanate C-N-lyase, cyanate hydratase, cyanate hydrolase, cyanate lyase, CYN, CynS, EC 3.5.5.3, EC 4.3.99.1, Hydrolase, cyanate, Ngar_c31480, NITMOv2_1274, OsCYN, slr0899, SpCynS, Spro_1533, tetur28g02430
ECTree
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Inhibitors
Inhibitors on EC 4.2.1.104 - cyanase
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ammonium
negative regulation even in the presence of cyanate. The negative effect exerted by ammonium on cyanate assimilation seems to take place at the level of gene expression, since the addition of ammonium to cells growing in cyanate had no effect on either cyanase activity or cyanate consumption
thiocyanate
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kinetics of cyanase activity at pH 7.5 and 37°C
partial auto-inhibition at high concentrations of potassium cyanate
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reversible inhibition which can be prevented by saturating concentrations of cyanate or bicarbonate
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reversible inhibition which can be prevented by saturating concentrations of cyanate or bicarbonate
oxalate
the membrane-impermeant inhibitor of cyanobacterial cyanase has minor effects on acid-labile or acid-stable fractions indicating the absence of cyanase from the periplasm
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reversible inhibition which can be prevented by saturating concentrations of cyanate or bicarbonate
the culture of Nitrososphaera gargensis grows well in the presence of 2 mM ammonium and growth is not inhibited by addition of 0.5 mM cyanate
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additional information
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the culture of Nitrososphaera gargensis grows well in the presence of 2 mM ammonium and growth is not inhibited by addition of 0.5 mM cyanate
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additional information
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in native cyanase the sulfhydryl group per se is not required for catalytic acivity, but it may play a role in stabilizing octameric structure, and that octameric structure is required for catalytic activity
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additional information
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free sulfhydryl groups are not required for catalytic activity, the catalytic activity may be dependent upon oligomeric structure
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additional information
the enzyme is insensitive to 10 mM thiocyanate, a competitive inhibitor of some cyanases
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