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2.5.1.154
Cobalamin
interaction of Co(II)cobalamin and cob(II)inamide (Co(II)Cbi+) with EutT in the absence and presence of cosubstrate ATP. EutT displays a similar substrate specificity as Salmonella enterica EutT and can bind both Co(II)cobalamin and Co(II)Cbi+ when complexed with MgATP, though it exclusively converts Co(II)cobalamin to a four-coordinate species. Listeria monocytogenes EutT achieves a more than 98% conversion yield of the five-coordinate to four-coordinate state on addition of just over one molar equivalent of cosubstrate MgATP
758818
2.5.1.154
Cobalamin
the reduced catalytic activity of EutT wild-type in complex with Co relative to the Fe(II)-containing enzyme arises from the incomplete incorporation of Co(II) ions and, thus, a decrease in the relative population of four-coordinate Co(II)Cbl. The Co(II) ions reside in a distorted tetrahedral coordination environment with direct cysteine sulfur ligation. Residues in the HX11CCX2C(83) motif are required for the tight binding of the divalent metal ion and are critical for the formation of a four-coordinate cob(II)alamin intermediate. Residue Cys80 coordinates to the Co(II) ion, while the additional residues are important for maintaining the structural integrity and/or high affinity of the metal binding site
762727
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