Enzymes
| UniProtKB help_outline | 13,684 proteins |
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Reaction participants Show >> << Hide
- Name help_outline ethanolamine Identifier CHEBI:57603 Charge 1 Formula C2H8NO InChIKeyhelp_outline HZAXFHJVJLSVMW-UHFFFAOYSA-O SMILEShelp_outline [NH3+]CCO 2D coordinates Mol file for the small molecule Search links Involved in 44 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline acetaldehyde Identifier CHEBI:15343 (CAS: 75-07-0) help_outline Charge 0 Formula C2H4O InChIKeyhelp_outline IKHGUXGNUITLKF-UHFFFAOYSA-N SMILEShelp_outline [H]C(C)=O 2D coordinates Mol file for the small molecule Search links Involved in 47 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline NH4+ Identifier CHEBI:28938 (CAS: 14798-03-9) help_outline Charge 1 Formula H4N InChIKeyhelp_outline QGZKDVFQNNGYKY-UHFFFAOYSA-O SMILEShelp_outline [H][N+]([H])([H])[H] 2D coordinates Mol file for the small molecule Search links Involved in 529 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:15313 | RHEA:15314 | RHEA:15315 | RHEA:15316 | |
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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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Cobalamin-dependent dehydratases and a deaminase: radical catalysis and reactivating chaperones.
Toraya T.
Adenosylcobalamin, a coenzyme form of vitamin B12, is an organometallic compound that participates in about ten enzymatic reactions. These enzymes catalyze chemically challenging reactions by using a highly reactive primary carbon radical that is derived from homolysis of the coenzyme Co-C bond. A ... >> More
Adenosylcobalamin, a coenzyme form of vitamin B12, is an organometallic compound that participates in about ten enzymatic reactions. These enzymes catalyze chemically challenging reactions by using a highly reactive primary carbon radical that is derived from homolysis of the coenzyme Co-C bond. Among them, diol dehydratases and ethanolamine ammonia-lyase have been most extensively studied to establish the general mechanism of adenosylcobalamin-assisted enzymatic catalysis and radical-catalyzed reactions. Another important point is that adenosylcobalamin-dependent radical enzymes are prone to mechanism-based irreversible inactivation during catalysis and have their own chaperones for the maintenance of catalytic activities. This review will highlight biochemical, structural, and computational studies with special emphases on radical catalysis and reactivating chaperones of these enzymes. << Less
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Ethanolamine deaminase, a cobamide coenzyme-dependent enzyme. I. Purification, assay, and properties of the enzyme.
Kaplan B.H., Stadtman E.R.
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The clostridial fermentations of choline and ethanolamine. II. Requirement for a cobamide coenzyme by an ethanolamine deaminase.
Bradbeer C.
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The clostridial fermentations of choline and ethanolamine. 1. Preparation and properties of cell-free extracts.
Bradbeer C.