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Literature summary 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 .
    View publication on PubMed

Cloned(Commentary)

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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.2.1.1 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

EC Number Inhibitors Comment Organism Structure
2.2.1.1 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
2.2.1.1 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

EC Number Metals/Ions Comment Organism Structure
2.2.1.1 Mg2+ 5 mM used in assay conditions Chlamydomonas reinhardtii
2.2.1.1 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]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.2.1.1 156000
-
 gel filtration Chlamydomonas reinhardtii

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
2.2.1.1 Chlamydomonas reinhardtii A8IAN1
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Subunits

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

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
2.2.1.1 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

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