Enzymes
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- Name help_outline (E)-2-(2-furyl)-3-(5-nitro-2-furyl)acrylamide Identifier CHEBI:15659 Charge 0 Formula C11H8N2O5 InChIKeyhelp_outline LYAHJFZLDZDIOH-SOFGYWHQSA-N SMILEShelp_outline NC(=O)C(=C\c1ccc(o1)[N+]([O-])=O)\c1ccco1 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline (Z)-2-(2-furyl)-3-(5-nitro-2-furyl)acrylamide Identifier CHEBI:15660 (CAS: 3688-53-7) help_outline Charge 0 Formula C11H8N2O5 InChIKeyhelp_outline LYAHJFZLDZDIOH-VURMDHGXSA-N SMILEShelp_outline NC(=O)C(=C/c1ccc(o1)[N+]([O-])=O)\c1ccco1 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:21848 | RHEA:21849 | RHEA:21850 | RHEA:21851 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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A cis-trans isomerising activity of Escherichia coli. Isomerization from 2-(2-furyl)-3-cis-(5-nitro-2-furyl) acrylamide (furylfuramide) to its trans isomer.
Tomoeda M., Kitamura R.
The soluble enzyme fraction derived from Escherichia coli K-12 JE2100 cells was found to exhibit, in addition to Nadh- and NADPH-dependent reductase activities, NADH-dependent cis-trans isomerising activity toward 2-(2-furyl-3-(5-nitro-2-furyl)acrylamide leading to a specific change in geometrical ... >> More
The soluble enzyme fraction derived from Escherichia coli K-12 JE2100 cells was found to exhibit, in addition to Nadh- and NADPH-dependent reductase activities, NADH-dependent cis-trans isomerising activity toward 2-(2-furyl-3-(5-nitro-2-furyl)acrylamide leading to a specific change in geometrical configuration of the vinyl group at the 2-position from cis to trans but not in the reverse direction. This furylfuramide-isomerising action of bacteria was dicoumarol insensitive, and did not require glutathione for full activity. The particulate enzyme fraction derived from JE2100 cells, although it showed little reductase activity toward furylfuramide in the presence of either NADH or NADPH, revealed an isomerising activity in the presence of NADH. << Less