Literature summary for 2.5.1.154 extracted from

Pallares, I.G.; Moore, T.C.; Escalante-Semerena, J.C.; Brunold, T.C.
Spectroscopic studies of the EutT adenosyltransferase from Salmonella enterica Evidence of a tetrahedrally coordinated divalent transition metal cofactor with cysteine ligation (2017), Biochemistry, 56, 364-375 .

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Protein Variants

Protein Variants	Comment	Organism
Cys79A	mutation in the HX11CCX2C(83) motif required for the tight binding of the divalent metal, substitution causes a large decrease in the affinity of EutT for Co(II)	Salmonella enterica subsp. enterica serovar Typhimurium
Cys80A	mutation in the HX11CCX2C(83) motif required for the tight binding of the divalent metal, inactive	Salmonella enterica subsp. enterica serovar Typhimurium
Cys83A	mutation in the HX11CCX2C(83) motif required for the tight binding of the divalent metal, large negative effect on enzyme activity, only capable of very slow turnover	Salmonella enterica subsp. enterica serovar Typhimurium
His67A	mutation in the HX11CCX2C(83) motif required for the tight binding of the divalent metal, at most 1% of the divalent metal sites are occupied	Salmonella enterica subsp. enterica serovar Typhimurium
His75A	mutation in the HX11CCX2C(83) motif required for the tight binding of the divalent metal, at most 1% of the divalent metal sites are occupied	Salmonella enterica subsp. enterica serovar Typhimurium

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Cobalt	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	Salmonella enterica subsp. enterica serovar Typhimurium

Organism

Organism	UniProt	Comment	Textmining
Salmonella enterica subsp. enterica serovar Typhimurium	Q9ZFV4	-	-

Synonyms

Synonyms	Comment	Organism
EutT	-	Salmonella enterica subsp. enterica serovar Typhimurium

Cofactor

Cofactor	Comment	Organism	Structure
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	Salmonella enterica subsp. enterica serovar Typhimurium

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Release 2023.1 (January 2023)