. 2014 Jan 8;53(3):601–609. doi: 10.1021/bi400931k

Table 1. Activities of WT PfTR and Mutant Enzymes of the C-Terminal β–Turn−β Motif with Various Substrates^a.

		mol of NADPH min^–1 (mol of TR)⁻¹
enzyme	PfTR	90 μM Trx	300 μM selenocystine	5 mM lipoic acid
PfTR-GC₁GGGKC₂G^b	1	500 ± 20	410 ± 30	90 ± 10
PfTRΔ7^c	2	ND^d	3 ± 0.2	140 ± 1
PfTR-GC₁GGGAC₂G^b	3	375 ± 20	350 ± 15	65 ± 5
PfTR-GC₁GGGKC₂^b	4	7 ± 0.5	185 ± 10	70 ± 3
PfTR-GC₁GGGKC₂GG^b	5	290 ± 10	400 ± 20	90 ± 2

In Tables 1–4, the main body of the enzyme is abbreviated as PfTR. The amino acid sequence of the C-terminal redox center is abbreviated with the one-letter amino acid codes representing the final seven C-terminal amino acids. Thus, the WT enzyme is abbreviated as PfTR-GC₁GGGKC₂G. Each of the mutants is denoted similarly with the mutant sequence of amino acids of the C-terminal redox center abbreviated with one-letter codes after the abbreviation PfTR.

Recombinant protein produced as a GST fusion.

Recombinant protein produced as an intein fusion.

No detectable activity.

Table 1. Activities of WT PfTR and Mutant Enzymes of the C-Terminal β–Turn−β Motif with Various Substratesa.

Table 1. Activities of WT PfTR and Mutant Enzymes of the C-Terminal β–Turn−β Motif with Various Substrates^a.