Skip to main content
. Author manuscript; available in PMC: 2008 Nov 21.
Published in final edited form as: J Am Chem Soc. 2007 Oct 31;129(46):14336–14347. doi: 10.1021/ja074650f

Table 1.

Kinetic Data for C-Glycosyltransferases MceC and IroBa

Ent MGE DGE lin-Ent lin-MGE UDP-Glce
MceC kcat (min−1) 2.7 ± 0.3 1.22 ± 0.05 n.d.b 0.61 ± 0.06c n.d. 1.19 ± 0.03
Km(μM) 0.94 ± 0.38 18.5 ± 2.4 n.d.b 17.8 ± 4.6c n.d. 87 ± 6
kcat/Km (min−1μM−1) 2.9 0.07 n.d. 0.03 n.d. 0.014
IroB kcat (min−1) 1.8 ± 0.1 5.1 ± 0.2 3.0 ± 0.1 0.57± 0.002 0.44 ± 0.03d n.d.
Km(μM) 2.0 ± 0.3 48 ± 6 72 ± 5 36 ±4 111 ± 15d n.d.
kcat/Km (min−1μM−1) 0.9 0.11 0.04 0.02 0.004 n.d.
a

Experiments were conducted at room temperature in buffer D (75 mM Tris-HCl pH 8, 5 mM MgCl2 and 2.5 mM TCEP) and in the presence of 500 μM UDP-Glc.

b

n.d. = not determined.

c

Substrate inhibition was observed at [lin-Ent] > 64 μM.

d

Substrate inhibition was observed at [lin-MGE] > 256 μM.

e

The UDP-Glc concentration was varied in the presence of 100 μM Ent.