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. 2003 Jul;132(3):1642–1651. doi: 10.1104/pp.103.020453

Table III.

Substrate specificity of β-Ala NMTase expressed in yeast (pYES-NMTase)

Relative activities are shown as percentage of that found with β-Ala. Specific activity with β-Ala (100%) was 105.2 nmol h–1 mg–1 protein. A protein extract from yeast (pYES-lacZ) was assayed as a negative control. ND, Not detectable. The minimum detectable activity was 10 pmol h–1 mg–1 protein. Values are means and se from triplicate assays.

Methyl Acceptor Substrate (10 mM) pYES-NMTase pYES-lacZ
β-Ala 100 ND
N-Methyl β-Ala 61.4 ± 0.34 ND
N,N-Dimethyl β-Ala 19.8 ± 0.22 ND
β-Alanyl Gly 0.39 ± 0.03 0.31 ± 0.01
DL-β-Aminoisobutryic acid 2.01 ± 0.13 0.31 ± 0.01
L-Ala 0.47 ± 0.12 0.21 ± 0.08
L-Pro ND 0.17 ± 0.04
trans-4-Hydroxy L-Pro ND ND
Gly 1.77 ± 0.04 0.9 ± 0.1
Putrescine 1.36 ± 0.11 1.61 ± 0.12
γ-Amino-n-butyric acid ND 1.15 ± 0.04
N-Methyl DL-Ala 0.65 ± 0.09 0.41 ± 0.02
N,N-Dimethyl Gly ND ND