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EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Reference
2.7.8.13
-999
-
more
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
-999
-
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
-999
-
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
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