5.4.99.2	(Cobeta-5'-Deoxyadenosine-5'-yl)-(p-cresolyl)cobamide	can serve as coenzyme, Km: 0.000064	3515	
5.4.99.2	adenosylcobalamin	required	677443	
5.4.99.2	hMMAA	hMCM loses activity during catalysis, but the interaction with human MMAA (hMMAA), a GTPase protein, avoids this loss or restores hMCM activity. Formation and accumulation of OH2Cbl, the oxidized form of cofactor AdoCbl formed during catalysis, is the cause of hMCM inactivation. The complex formation of hMCM/hMMAA decreases the rate of oxidized cofactor formation, protecting the hMCM enzyme. hMMAA is able to remove the damaged cofactor through GTP hydrolysis.a modification in the kinetic parameters of hMCM in presence of hMMAA is observed. No activity is recovered in the presence of hMMAAwith GMPPNP, confirming the need of GTP hydrolysis for this cofactor removal. In vivo localization of hMMAA and its colocalization with hMCM in human fibroblasts mitochondria. hMMAAis localized in both the cytoplasm and mitochondria but in less abundance and distribution than enzyme hMCM	747209	
5.4.99.2	hydroxocobalamin	supplementation of hydroxocobalamin results in a marked increase in the holo-MCM activity in a dose-dependent manner, although the holo-MCM activity does not exceed 30% of the total-MCM activity even if hydroxocobalamin is supplemented at 10 mM	691535	
5.4.99.2	methylmalonic acidemia protein	after 60 min of reaction, when MCM is inactive, the addition of methylmalonic acidemia protein increases the enzymatic activity through GTP hydrolysis, indicating reactivation of MCM by exchange of the damaged cofactor. Methylmalonic acidemia protein acts as a chaperone of human MCM	714049