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Literature summary for 1.14.99.48 extracted from

  • Ukpabi, G.; Takayama, S.J.; Mauk, A.G.; Murphy, M.E.
    Inactivation of the heme degrading enzyme IsdI by an active site substitution that diminishes heme ruffling (2012), J. Biol. Chem., 287, 34179-34188.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
mutant W66Y in complex with heme and its cyanide-bound form. Heme binds to the mutant with less heme ruffling than observed for wild-type IsdI. The reduction potential of the variant (-96 mV versus standard hydrogen electrode) is similar to that of wild-type IsdI (-89 mV) Staphylococcus aureus

Protein Variants

Protein Variants Comment Organism
W66A Trp66 is a conserved heme pocket residue implicated in heme ruffling. Mutant is inactive Staphylococcus aureus
W66F Trp66 is a conserved heme pocket residue implicated in heme ruffling. Mutant shows about half of wild-type heme degradation activity Staphylococcus aureus
W66L Trp66 is a conserved heme pocket residue implicated in heme ruffling. Mutant is inactive Staphylococcus aureus
W66Y Trp66 is a conserved heme pocket residue implicated in heme ruffling. Mutant shows about half of wild-type heme degradation activity Staphylococcus aureus

Organism

Organism UniProt Comment Textmining
Staphylococcus aureus Q7A827
-
-
Staphylococcus aureus N315 Q7A827
-
-

Synonyms

Synonyms Comment Organism
isdG
-
Staphylococcus aureus