NDLI: Isolation and properties of human transketolase

Content Provider	Springer Nature Link
Author	Meshalkina, L. E. Solovjeva, O. N. Khodak, Yu. A. Drutsa, V. L. Kochetov, G. A.
Copyright Year	2010
Abstract	Recombinant human (His)6-transketolase (hTK) was obtained in preparative amounts by heterologous expression of the gene encoding human transketolase in Escherichia coli cells. The enzyme, isolated in the form of a holoenzyme, was homogeneous by SDS-PAGE; a method for obtaining the apoenzyme was also developed. The amount of active transketolase in the isolated protein preparation was correlated with the content of thiamine diphosphate (ThDP) determined in the same preparation. Induced optical activity, facilitating studies of ThDP binding by the apoenzyme and measurement of the transketolase reaction at each stage, was detected by circular dichroism spectroscopy. A single-substrate reaction was characterized, catalyzed by hTK in the presence of the donor substrate and in the absence of the acceptor substrate. The values of the Michaelis constant were determined for ThDP and a pair of physiological substrates of the enzyme (xylulose 5-phosphate and ribose 5-phosphate).
Starting Page	873
Ending Page	880
Page Count	8
File Format	PDF
ISSN	00062979
Journal	Biochemistry (Moscow)
Volume Number	75
Issue Number	7
e-ISSN	16083040
Language	English
Publisher	SP MAIK Nauka/Interperiodica
Publisher Date	2010-07-20
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	human transketolase thiamine diphosphate induced optical activity circular dichroism spectroscopy Biomedicine general Microbiology Bioorganic Chemistry Biochemistry
Content Type	Text
Resource Type	Article
Subject	Biochemistry Biophysics Geriatrics and Gerontology

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Influence of donor substrate on kinetic parameters of thiamine diphosphate binding to transketolase

New function of the amino group of thiamine diphosphate in thiamine catalysis

Effect of Transketolase Substrates on Holoenzyme Reconstitution and Stability

Interaction of transketolase from human tissues with substrates

Computer modeling of transketolase-like protein, TKTL1, a marker of certain tumor tissues

Two methods for determination of transketolase activity

Expression, purification, and secondary structure characterization of recombinant KCTD1

Inhibition of transketolase by hexacyanoferrate(III)

Monitoring protein folding and unfolding pathways through surface hydrophobicity changes using fluorescence and circular dichroism spectroscopy

Isolation and properties of human transketolase

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