2.1.1.10	additional information	-	structural comparison and enzymatic properties of purified human betaine-homocysteine methyltransferase (BHMT, EC 2.1.1.5) and human betaine-homocysteine methyltransferase-2 (BHMT-2) determined, methylation capacities of homocysteine analyzed, S-adenosyl-L-methionine-dependent methylation of homocysteine predicted mostly occurs via BHMT-2 in vivo	687808	
2.1.1.10	0.0008	-	kidney, S-methyl-L-methionine as methyl donor	441384	
2.1.1.10	0.0009	-	using L-selenocysteine as substrate	676384	
2.1.1.10	0.0017	-	using DL-selenocysteine as substrate	676384	
2.1.1.10	0.0022	-	liver, S-adenosyl-L-methionine as methyl donor	441384	
2.1.1.10	0.0044	-	mutant K10A, pH 7.5, 37°C	756095	
2.1.1.10	0.0047	-	mutant K8A, pH 7.5, 37°C	756095	
2.1.1.10	0.0054	-	using L-cysteine as substrate	676384	
2.1.1.10	0.0087	-	liver, S-methyl-L-methionine as methyl donor	441384	
2.1.1.10	0.0109	-	mutant K7A, pH 7.5, 37°C	756095	
2.1.1.10	0.012	-	S-methyl-L-methionine as methyl donor	441384	
2.1.1.10	0.01215	-	wild-type, pH 7.5, 37°C	756095	
2.1.1.10	0.014	-	S-methyl-L-methionine as methyl donor	441384	
2.1.1.10	0.0147	-	using DL-cysteine as substrate	676384	
2.1.1.10	0.017	-	S-methyl-L-methionine as methyl donor	441384	
2.1.1.10	0.0936	-	using DL-homocysteine as substrate	676384	
2.1.1.10	0.164	-	crude extract, pH 7.2, 37°C	756423	
2.1.1.10	1.37	-	purified enzyme, S-adenosyl-L-methionine as methyl donor	441385