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Ligand 1-cyclohexyl-3-(2-morpholinoethyl)-carbodiimide metho-p-toluenesulfonate Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Basic Ligand Information Molecular Structure
C2 1 H3 4 N3 O4 S
1-cyclohexyl-3-(2-morpholinoethyl)-carbodiimide metho-p-toluenesulfonate
GBCAVSYHPPARHX-UHFFFAOYSA-M
1-cyclohexyl-3-(2-morpholinoethyl)-carbodiimide metho-p-toluenesulphonate, 1-cyclohexyl-3-(2-morpholinoethyl)carbodiimide metho-p-toluenesulfonate, 1-cyclohexyl-3-(2-morpholinoethyl)carbodiimide metho-p-toluene sulfonate, N-cyclohexyl-N'-[2-(N-methylmorpholino)-ethyl]carbodiimide p-toluene sulfonate
Roles as Enzyme Ligand
Inhibitor in Enzyme-catalyzed Reactions (6 results)
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1.5 mM, 68% inhibition, hydroxylamine protects
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preincubation with NO2- completely protects
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complete inactivation at 22 mM
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20 mM, 99.6% inhibition
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reacts with Asp and Glu residues, causes a slight decrease in activity
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Enzyme Kinetic Parameters
References & Links Literature References (5)
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Porcine thyroid fucosidase
1981
Grove, D.S.; Serif, G.S.
Biochim. Biophys. Acta
662
246-255
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Some properties of nitrite and hydroxylamine reductases from Derxia gummosa
1986
Wang, R.; Nicholas, D.J.D.
Phytochemistry
25
2463-2469
Sulfite oxidase from chicken liver. Further characterization of the role of carboxyl groups in the reaction with cytochrome c
1988
Ritzman, M.; Bosshard, H.R.
Eur. J. Biochem.
172
377-381
Some molecular and inhibitory specifications of a dipeptidyl carboxypeptidase from the polychaete Neanthes virens resembling angiotensin I converting enzyme
2000
Kawamura, T.; Kikuno, K.; Oda, T.; Muramatsu, T.
Biosci. Biotechnol. Biochem.
64
2193-2200
Primary structure and chemical modification of some amino acid residues of bifunctional alginate lyase from a marine bacterium Pseudoalteromonas sp. strain no. 272
2002
Iwamoto, Y.; Iriyama, K.; Osatomi, K.; Oda, T.; Muramatsu, T.
J. Protein Chem.
21
455-463
Links to other databases for 1-cyclohexyl-3-(2-morpholinoethyl)-carbodiimide metho-p-toluenesulfonate