1.14.11.1	drug target	inhibitors of gamma-butyrobetaine hydroxylase 1 (BBOX1) could be a potential therapeutic option for Triple-negative breast cancer	765384	
1.14.11.1	evolution	comparison of properties, substrate specificities, and structures of the human enzyme (PDB ID 3O2G) and the enzyme from Pseudomonas sp. AK1, detailed overview	-, 745953	
1.14.11.1	evolution	the enzyme belongs to the 2-oxoglutarate/Fe(II) dependent oxygenase family	-, 744503, 744717, 745684	
1.14.11.1	evolution	the enzyme belongs to the superfamily of Fe(II) and 2OG dependent dioxygenases	744690	
1.14.11.1	evolution	the GBBH residues involved in zinc binding are evolutionary conserved in all sequenced eukaryotes more complex than Caenorhabditis elegans	711108	
1.14.11.1	metabolism	gamma-butyrobetaine hydroxylase (BBOX) catalyses the final step in the biosynthesis of carnitine i.e. the stereoselective hydroxylation of gamma-butyrobetaine (GBB)	-, 745953	
1.14.11.1	metabolism	gamma-butyrobetaine hydroxylase (BBOX) catalyses the final step of carnitine biosynthesis	744690	
1.14.11.1	metabolism	last limiting enzyme of the L-carnitine biosynthesis pathway and plays an important role in catalyzing the hydroxylation of gamma-butyrobetaine to L-carnitine	763867	
1.14.11.1	metabolism	the enzyme catalyses the second, essential step of carnitine biosynthesis	744503	
1.14.11.1	metabolism	the enzyme catalyzes the final step in the biosynthesis of L-carnitine in humans	764457