. 2014 Dec 19;9(12):e116355. doi: 10.1371/journal.pone.0116355

Table 2. Aldolase and transaldolase activities reported in Archaea.

Organism	Assay	Specific activity (mU mg Protein^-1)			Reference
		ORF	Substrate	activity
M. jannaschii	⁽¹⁾coupled assay, recombinant proteins	⁽⁴⁾ MJ0400, ⁽⁵⁾ MJ1585	F-1,6-P	<0.1, 540	[25]
M. maripaludis	⁽¹⁾ coupled assay, cell extract	WT, ⁽⁴⁾ ΔMMP0686	F-1,6-P	6.6-7.2, 6.6-7.2	[25]
M. jannaschii	⁽²⁾ GC-MS, recombinant proteins	⁽⁴⁾ MJ0400+ ⁽⁶⁾ MJ1249, MJ0400+MJ1249+NADP, MJ0400+MJ1249+NAD	ASA+DKFP	4.8, 103.1, 226.8	[6]
H. salinarum	⁽³⁾ colorimetric assay, recombinant proteins	⁽⁴⁾ OE1472F, ⁽⁵⁾ OE2019F	F-1,6-P	71, 78	This study
⁽⁷⁾ T. tenax	⁽¹⁾ coupled assay, recombinant proteins	AJ310483 ⁽⁹⁾	F-1,6-P	230	[10]
⁽⁸⁾ P. furiosus	⁽¹⁾ coupled assay, recombinant proteins	AF368259 ⁽⁹⁾	F-1,6-P	580	[10]

⁽¹⁾

In the coupled assay, aldolase activity was determined using coupled assay, were the cleavage of F-1,6-P was coupled with glycerol-3-phosphate dehydrogenase (EC 1.1.1.8) and triose-phosphate isomerase (TIM, EC 5.3.1.1) of rabbit muscle. Enzymatic activities were measured by monitoring the increase in absorption of NADH at 366 nm (ε_50°C = 3.36 mm ⁻¹cm⁻¹).

⁽²⁾

DHQ generated with recombinant proteins was determined by GC-MS.

⁽³⁾

Formation of DHAP was measured by Colorimetric assay (see materials and methods for details).

⁽⁴⁾

MJ0400 from M. jannaschii is homologous to OE1472F from H. salinarum and MMP0686 from M. maripaludis. Predicted transaldolase catalyzing the first reaction of the AroAA biosynthesis pathway in these organisms.

⁽⁵⁾

MJ1585 from M. jannaschii is homologous to OE2019F from H. salinarum and MMP0293 from M. maripaludis. It is an aldolase.

⁽⁶⁾

MJ1249 is homologous to OE1475F from H. salinarum and MMP0006 from M. maripaludis. It is believed to catalyze the second reaction in the AroAA biosynthesis, synthesizing DHQ.

⁽⁷⁾

Thermoproteus tenax, crenarchaeon,

⁽⁸⁾

Pyrococcus furiosus, euryarchaeon.

⁽⁹⁾

GenBank accession number.