Literature summary for 2.2.1.1 extracted from

Pasquini, M.; Fermani, S.; Tedesco, D.; Sciabolini, C.; Crozet, P.; Naldi, M.; Henri, J.; Vothknecht, U.; Bertucci, C.; Lemaire, S.D.; Zaffagnini, M.; Francia, F.
Structural basis for the magnesium-dependent activation of transketolase from Chlamydomonas reinhardtii (2017), Biochim. Biophys. Acta, 1861, 2132-2145 .

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Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli BL21 cells	Chlamydomonas reinhardtii

Crystallization (Commentary)

Crystallization (Comment)	Organism
apoenzyme and enzyme in complex with thiamine diphosphate and Mg2+, hanging drop vapor diffusion method, using 10% (w/v) PEG 6K, 5 % (v/v) 2-m,ethyl-2,4-pentanediol and 0.1 M MES pH 6.5-7.0 or 0.1 M HEPES pH 7.0-8.0	Chlamydomonas reinhardtii

Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	after 3 h incubation with 50 mM oxidized dithiothreitol, the activity of the enzyme bound to thiamine diphosphate and Mg2+ is almost unaffected, retaining more than 90% of the control (reduced) enzyme activity	Chlamydomonas reinhardtii
oxidized dithiothreitol	in the absence of Mg2+, the enzyme is strongly inhibited by oxidation, retaining 20-30 % of its control activity when exposed to 50 mM oxidized dithiothreitol. The apoenzyme is 80% inactivated following incubation in the presence of identical amount of oxidized dithiothreitol	Chlamydomonas reinhardtii

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	5 mM used in assay conditions	Chlamydomonas reinhardtii
Mg2+	the enzyme attains its full activation at Mg2+ concentration of equal or more than 1 mM. 15 mM used in assay conditions. Mg2+ is fundamental to allow gradual conformational arrangements suited for optimal catalysis. Moreover, Mg2+ is involved in the control of redox sensitivity of the enzyme	Chlamydomonas reinhardtii

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
156000	-	gel filtration	Chlamydomonas reinhardtii

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate	Chlamydomonas reinhardtii	-	D-ribose 5-phosphate + D-xylulose 5-phosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Chlamydomonas reinhardtii	A8IAN1	-	-

Purification (Commentary)

Purification (Comment)	Organism
Ni-NTA column chromatography	Chlamydomonas reinhardtii

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate	-	Chlamydomonas reinhardtii	D-ribose 5-phosphate + D-xylulose 5-phosphate	-	?

Subunits

Subunits	Comment	Organism
homodimer	x * 75170, mass spectrometry	Chlamydomonas reinhardtii

Temperature Range [°C]

Temperature Minimum [°C]	Temperature Maximum [°C]	Comment	Organism
37	45	the apoenzyme shows 50% activity at 37°C while this value is shifted to about 45°C for enzyme bound to thiamine diphosphate and Mg2+	Chlamydomonas reinhardtii

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	-	Chlamydomonas reinhardtii
thiamine diphosphate	dependent on	Chlamydomonas reinhardtii

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Release 2023.1 (January 2023)