PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
24330302-7	2013	The observed homozygous p.P86L mutation in the N-terminal extended segment may yield reduced MCM activity and is refractory to hydroxocobalamin supplementation, while not inducing a metabolically unstable phenotype.	Hydroxocobalamin	127-143	methylmalonyl-CoA mutase	Homo sapiens	93-96	
7909321-1	1994	The mut0 mutation resulting in methylmalonyl CoA mutase (MCM) apoenzyme deficiency and methylmalonic aciduria is characterized by undetectable enzyme activity in cell extracts and low incorporation of propionate into cultured cells which is not stimulated by hydroxycobalamin.	Hydroxocobalamin	259-275	methylmalonyl-CoA mutase	Homo sapiens	57-60	
36882-1	1979	We have examined the effect of addition of hydroxocobalamin to growth medium on the activity of the adenosylcobalamin-requiring enzyme methylmalonyl CoA mutase in normal human fibroblasts and in mutant human fibroblasts derived from patients with inherited methylmalonicacidemia.	Hydroxocobalamin	43-59	methylmalonyl-CoA mutase	Homo sapiens	135-159