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Literature summary for 1.14.99.48 extracted from

  • Wu, R.; Skaar, E.P.; Zhang, R.; Joachimiak, G.; Gornicki, P.; Schneewind, O.; Joachimiak, A.
    Staphylococcus aureus IsdG and IsdI, heme-degrading enzymes with structural similarity to monooxygenases (2005), J. Biol. Chem., 280, 2840-2846.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
to 1.5 A resolution. Structure of the enzyme resembles the ferredoxin-like fold and forms a beta-barrel at the dimer interface. Two large pockets found on the outside of the barrel contain the putative active sites Staphylococcus aureus

Protein Variants

Protein Variants Comment Organism
F23A mutation does not significantly affect heme binding or degradation Staphylococcus aureus
H77A mutation abolishes IsdG-mediated heme degradation Staphylococcus aureus
L17A mutation does not significantly affect heme binding or degradation Staphylococcus aureus
M38A slight reduction of heme degradation, mutation shifts the peak absorbance of the Soret band to 430 nm Staphylococcus aureus
N7A mutation abolishes IsdG-mediated heme degradation Staphylococcus aureus
S70A mutation does not significantly affect heme binding or degradation Staphylococcus aureus
W67A mutation abolishes IsdG-mediated heme degradation Staphylococcus aureus

Organism

Organism UniProt Comment Textmining
Staphylococcus aureus Q8NX62 isoform IsdG
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Staphylococcus aureus Q99X56 isoform IsdI
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Staphylococcus aureus ATCC 700699 Q99X56 isoform IsdI
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Staphylococcus aureus MW2 Q8NX62 isoform IsdG
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