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Literature summary for 1.13.11.54 extracted from

  • Chai, S.C.; Ju, T.; Dang, M.; Beaulieu Goldsmith, R.; Maroney, M.J.; Pochapsky, T.C.
    Characterization of metal binding in the active sites of acireductone dioxygenase isoforms from Klebsiella ATCC 8724 (2008), Biochemistry, 47, 2428-2438.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Klebsiella oxytoca

Protein Variants

Protein Variants Comment Organism
D101A about 60% of wild-type activity Klebsiella oxytoca
E100A about 2% of wild-type activity. E100 is not essential for metal binding Klebsiella oxytoca
E102A no catalytic activity Klebsiella oxytoca
E95A about 4% of wild-type activity Klebsiella oxytoca
H140A no catalytic activity Klebsiella oxytoca
H140F no catalytic activity Klebsiella oxytoca
H96A no catalytic activity Klebsiella oxytoca
H98A no catalytic activity Klebsiella oxytoca
H98S no catalytic activity. Mutant exhibits little affinity for either Ni2+ or Fe2+, indicating that His 98 is likely involved in binding both metals Klebsiella oxytoca

Metals/Ions

Metals/Ions Comment Organism Structure
Iron ligands are H96, H98, E102 and H140, the same as in the isoform requiring Ni2+, EC 1.13.11.54. Structural and functional differences between FeARD' and NiARD' forms are triggered by subtle differences in the local backbone. Both enzymes bind their respective metals with pseudo-octahedral geometry and both may lose a His ligand upon binding of substrate under anaerobic conditions Klebsiella oxytoca

Organism

Organism UniProt Comment Textmining
Klebsiella oxytoca Q9ZFE7
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Klebsiella oxytoca ATCC 8724 Q9ZFE7
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