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