BiSSCat Search in
Home Help FGROUP SUBSTRUCTURE compound enzyme Multiple

F411000 Primary amine

CLASS: Nitrogen / Amine COMPOUND: 20820 KEGG: 1553 NCI: 19267 ENZYME: 460 (Show enzyme(s)) RELATED: 5 F410000 Amine F411100 Mono-alkyl amine F411110 Alpha-amino acid F411200 Enamine F411400 Aniline

of 2083. [Next][Prev]

911. C12062 Naphthyl dipeptide (Molfile)(InChI)(KEGG)
No enzymes registered.

912. C11302 S-Octyl GSH (Molfile)(InChI)(KEGG)
No enzymes registered.

913. C02863 O-D-Mannosylprotein (Molfile)(InChI)(KEGG)
  • 2.4.1.109 dolichyl-phosphate-mannose-protein mannosyltransferase

914. C05681 Ceramide 2-aminoethylphosphonate (Molfile)(InChI)(KEGG)

915. C02010 Blasticidin S (Molfile)(InChI)(KEGG)

916. C01969 Xanthommatin (Molfile)(InChI)(KEGG)

917. C06870 Carbidopa-levodopa (Molfile)(InChI)(KEGG)
No enzymes registered.

918. C03860 Deaminohydroxyblasticidin S (Molfile)(InChI)(KEGG)

919. C00068 Thiamine diphosphate (Molfile)(InChI)(KEGG)
  • 1.2.1.58 phenylglyoxylate dehydrogenase (acylating)
  • 1.2.2.2 pyruvate dehydrogenase (cytochrome)
  • 1.2.3.3 pyruvate oxidase
  • 1.2.4.1 pyruvate dehydrogenase (acetyl-transferring)
  • 1.2.4.2 oxoglutarate dehydrogenase (succinyl-transferring)
  • 1.2.4.4 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)
  • 2.2.1.1 transketolase
  • 2.2.1.3 formaldehyde transketolase
  • 2.2.1.4 acetoin-ribose-5-phosphate transaldolase
  • 2.2.1.5 2-hydroxy-3-oxoadipate synthase
  • 2.2.1.6 acetolactate synthase
  • 2.7.4.15 thiamine-diphosphate kinase
  • 2.7.4.16 thiamine-phosphate kinase
  • 2.7.6.2 thiamine diphosphokinase
  • 3.6.1.28 thiamine-triphosphatase
  • 4.1.1.1 pyruvate decarboxylase
  • 4.1.1.47 tartronate-semialdehyde synthase
  • 4.1.1.7 benzoylformate decarboxylase
  • 4.1.1.71 2-oxoglutarate decarboxylase
  • 4.1.1.75 5-guanidino-2-oxopentanoate decarboxylase
  • 4.1.1.8 oxalyl-CoA decarboxylase
  • 4.1.2.38 benzoin aldolase
  • 4.1.2.9 phosphoketolase

920. C03476 5,12-Dihydroxanthommatin (Molfile)(InChI)(KEGG)
of 2083. [Next][Prev]

BiSSCat v1.06.20 http://bisscat.org/
Developed by Masaaki Kotera, Department of Biochemistry, Trinity College Dublin.
Science Foundation of Ireland is gratefully acknowledged.