Fig. 4: Analysis of CrmG catalyzing PLP amination with excess amino donor. | Communications Biology

Fig. 4: Analysis of CrmG catalyzing PLP amination with excess amino donor.

From: Structural studies reveal flexible roof of active site responsible for ω-transaminase CrmG overcoming by-product inhibition

Fig. 4: Analysis of CrmG catalyzing PLP amination with excess amino donor.

a UV–vis spectrophotometry analysis of CrmG catalyzing PLP conversion to PMP with excess amino donor (l-Glu, l-Gln, or l-Ala). b UV–vis spectrophotometry analysis of CrmG W223A mutant catalyzing PLP conversion to PMP with excess amino donor (l-Glu, l-Gln, or l-Ala). The assays were conducted in 1 mL of reaction mixture in Tris-HCl buffer (50 mM Tris pH 7.5, 0.1 M NaCl, 5% Glycerol), comprising of 0.02 mM CrmG or CrmG W223A mutant, 0.2 mM PLP, and 2 mM amino donor (l-Glu, l-Gln, or l-Ala).

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