EC Number   |
General Information |
Reference |
|---|
  2.5.1.154 | metabolism |
adenosyltransferase enzymes lower the thermodynamic barrier of the Co2+ to Co+ reduction needed for the formation of the organometalic Co-C bond of adenosylcobalamin. Cobalamin reductases identified thus far are most likely electron transfer proteins, not enzymes |
763244 |
| 2.5.1.154 | metabolism |
EutT converts cob(II)alamin to an effectively four-coordinate Co(II) species so as to facilitate Co(II) to Co(I) reduction. The mechanism for bond dissociation involves binding of the nucleotide loop of Co(II)Cbl to a site remote from the Co(II) center. EutT fails to promote axial ligand dissociation for the substrate analogue cob(II)inamide, a natural precursor of cob(II)alamin. EutT can adenosylate complete and incomplete Co(I)rrinoids |
762599 |
| 2.5.1.154 | physiological function |
during the synthesis of adenosylated corrinoids, reduction of co(II)rrinoids occurs on the adenosyltransferase enzyme once it has complexed with its substrate and ATP |
763197 |
| 2.5.1.154 | physiological function |
in Salmonlella typhimurium, three types of corrinoid adenosyltransferases have been described. CoBa is a housekeeping enzyme involved in both the de novo biosynthesis and the salvage of adenosylcobalamin. The PduO adenosyl transferase is encoded in an operon (pdu) for cobalamin-dependent propanediol degradation and is induced by propanediol. Transferase EutT is encoded within the operon for ethanolamine utilization (eut). CobA produces sufficient Ado-B12 to initiate eut operon induction and to serve as a cofactor for EA-lyase when B12 levels are high. Once the eut operon is induced, the EutT transferase supplies more Ado-B12 during the period of high demand |
763200 |
| 2.5.1.154 | physiological function |
lack of corrinoid adenosyltransferase CobA, Ec 2.5.1.17, and EutT blocks ethanolamine utilization. EutT is necessary and sufficient for growth of an Salmonella typhimurium CobA EutT mutant strain on ethanolamine as a carbon and energy or nitrogen source. Cell extracts enriched for EutT protein contain strong, readily detectable ATP:co(I)rrinoid adenosyltransferase activity. The activity is only detected in extracts maintained under anoxic conditions |
763199 |
