Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Klebsiella sp. |
Protein Variants | Comment | Organism |
---|---|---|
D101A | about 60% of wild-type activity | Klebsiella sp. |
E100A | about 2% of wild-type activity. E100 is not essential for metal binding | Klebsiella sp. |
E102A | no catalytic activity | Klebsiella sp. |
E95A | about 4% of wild-type activity | Klebsiella sp. |
H140A | no catalytic activity | Klebsiella sp. |
H140F | no catalytic activity | Klebsiella sp. |
H96A | no catalytic activity | Klebsiella sp. |
H98A | no catalytic activity | Klebsiella sp. |
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 sp. |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Nickel | ligands are H96, H98, E102 and H140, the same as in the isoform requiring Fe2+, 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 sp. |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Klebsiella sp. | - |
strain ATCC 8724 | - |