2.7.8.13	additional information	-	additional information	the enzyme exhibits Michaelis-Menten kinetics towards the heptaprenyl phosphate and dodecaprenyl phosphate lipid substrates. The catalytic constants kcat are 295/min and 54/min, respectively. The kcat for heptaprenyl phosphate is by 6fold lower than those determined for the longer-chain length lipids undecaprenyl phosphate and dodecaprenyl phosphate with 340/min and 295/min, respectively	737788	
2.7.8.13	additional information	-	UDP-N-acetylmuramoyl-pentapeptide	11fold increase in kcat for mutant D98N at pH 9.4 (ca. 0.0083 1/sec) compared to pH 7.2	690996	
2.7.8.13	additional information	-	undecaprenyl phosphate	11fold increase in kcat for mutant D98N at pH 9.4 (ca. 0.0083 1/sec) compared to pH 7.2	690996	
2.7.8.13	0.00005	-	UDP-N-acetylmuramoyl-pentapeptide	mutant H289R	690996	
2.7.8.13	0.00005	-	undecaprenyl phosphate	mutant H289R	690996	
2.7.8.13	0.00083	-	UDP-N-acetylmuramoyl-pentapeptide	mutant D99N	690996	
2.7.8.13	0.00083	-	undecaprenyl phosphate	mutant D99N	690996	
2.7.8.13	0.00117	-	UDP-N-acetylmuramoyl-pentapeptide	mutant D98N	690996	
2.7.8.13	0.00117	-	undecaprenyl phosphate	mutant D98N	690996	
2.7.8.13	0.0015	-	UDP-N-acetylmuramoyl-pentapeptide	mutant K116Q	690996