EC Number |
Protein Variants |
Reference |
---|
2.7.7.62 | D101G |
in vitro activity relative to wild-type: 71%, monomer/dimer ratio: 34/66 |
724319 |
2.7.7.62 | D83G |
in vitro activity relative to wild-type: 100%, monomer/dimer ratio: 82/18 |
-, 724319 |
2.7.7.62 | E18D |
in vitro activity relative to wild-type: 56%, monomer/dimer ratio: 40/60 |
724319 |
2.7.7.62 | G153D |
crystal structure of mutant is determined at 2.8 A: The protein crystallizes in the hexagonal space group P31 with 4 chains in the asymmetric unit. Mutant shows reduced activity and is composed of a monomer. Results from isothermal titration calorimetry experiments show that MjCobYG153D has 10fold higher affinity for GTP than wild-type, but fails to bind the corrinoid substrate |
724319 |
2.7.7.62 | G153D |
in vitro activity relative to wild-type: 2%, monomer/dimer ratio: 54/46 |
724319 |
2.7.7.62 | G153D |
residues R13 and K19 of the mutant directly coordinate the phosphate group of GTP in the X-ray structure. The X-ray structure of the CobYG153D:GTP complex is modeled as a homodimer |
-, 739433 |
2.7.7.62 | G8D |
mutant non-functional, monomer/dimer ratio: 33/67 |
724319 |
2.7.7.62 | H45A |
site-directed mutagenesis |
644438 |
2.7.7.62 | H45A/H46A |
site-directed mutagenesis |
644438 |
2.7.7.62 | H46A |
site-directed mutagenesis |
644438 |