Skip to main content
. 2021 Dec 23;12(1):11. doi: 10.3390/metabo12010011

Table 1.

Enzyme activity of PRISEs from A. thaliana. The kinetic constants for the cosubstrate were determined using progesterone as the substrate.

Enzyme (Substrate) Km
(µM)
kcat
(s−1)
Catalytic Efficiency
(s−1 M−1)
rAtStR2
rAtStR2 (progesterone) 64.7 0.15 2314
rAtStR2 (MVK) 157.5 0.03 163
rAtStR2 (NADPH2) 41.0 0.12 2927
Other PRISEs of cluster II
rEcP5βR2 (progesterone) a 82 0.05 552
rEcP5βR2 (MVK) a 224 0.05 245
rCrP5βR6 (progesterone) a 75.5 0.40 5530
rCrP5βR6 (MVK) a 118 0.03 261
rAtStR1 and rAtSt5βR1_F153A_F342A
rAtStR1 (progesterone) b 124.8 0.28 2244
rAtStR1 (MVK) b 75.5 0.20 7299
rAtStR1_F153A_F342A (progesterone) c 217 2.00 9218
rAtStR1_F153A_F342A (MVK) c - n.a. -
Other PRISEs of cluster I
rEcP5βR1 (progesterone) b 77 0.01 31
rEcP5βR1 (MVK) b 344 0.72 2143
rCrP5βR4 (progesterone) b 153 0.02 123
rCrP5βR4 (MVK) b 123 0.20 1562
Other MVK-converting enzymes
AtAER (MVK) d 55.0 83.0 1,500,000
AtAOR (MVK) e 2880 74.0 25,700

a [7]; b [9]; c [10]; d [26]; e [27]. n.a. = not accepted as substrate; n > 3.