Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.5.1.154 extracted from

  • Stracey, N.G.; Costa, F.G.; Escalante-Semerena, J.C.; Brunold, T.C.
    Spectroscopic study of the EutT adenosyltransferase from Listeria monocytogenes evidence for the formation of a four-coordinate cob(II)alamin intermediate (2018), Biochemistry, 57, 5088-5095 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.5.1.154

Metals/Ions

Metals/Ions Comment Organism Structure
additional information enzyme does not require a divalent metal cofactor for catalytic activity Listeria monocytogenes serotype 1/2a

Organism

Organism UniProt Comment Textmining
Listeria monocytogenes serotype 1/2a A0A0H3GFM5
-
-
Listeria monocytogenes serotype 1/2a 10403S A0A0H3GFM5
-
-

Synonyms

Synonyms Comment Organism
EutT
-
 Listeria monocytogenes serotype 1/2a
LMRG_00627
-
 Listeria monocytogenes serotype 1/2a

Cofactor

Cofactor Comment Organism Structure
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 Listeria monocytogenes serotype 1/2a