L-Threonine dehydrogenase (TDH) fromT. kodakaraensis, an enzyme involved in amino acid metabolism

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Crystallization and preliminary X-ray diffraction analysis of L-threonine dehydrogenase (TDH) from the hyperthermophilic archaeon Thermococcus kodakaraensis.

The enzyme L-threonine dehydrogenase catalyses the NAD(+)-dependent conversion of L-threonine to 2-amino-3-ketobutyrate, which is the first reaction of a two-step biochemical pathway involved in the metabolism of threonine to glycine. Here, the crystallization and preliminary crystallographic analysis of L-threonine dehydrogenase (Tk-TDH) from the hyperthermophilic organism Thermococcus kodakar...

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Rat liver L-threonine dehydrogenase.

L-threonine dehydrogenase (E.C.1.1.1.103) catalyzes the NAD+-dependent transformation of Lthreonine to 2-amino 3-0x0-butyric acid, which spontaneously loses CO2 with the final production of aminoacetone ( 1) The enzyme is present in several microorganisms as well as in the liver of vertebrates (2-6). We studied some properties of the rat liver enzyme, showing that the activity was strongly inhi...

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An Evolutionary Relationship Between Stearoyl-CoA Desaturase (SCD) Protein Sequences Involved in Fatty Acid Metabolism

Background: Stearoyl-CoA desaturase (SCD) is a key enzyme that converts saturated fatty acids (SFAs) to monounsaturated fatty acids (MUFAs) in fat biosynthesis. Despite being crucial for interpreting SCDs’ roles across species, the evolutionary relationship of SCD proteins across species has yet to be elucidated. This study aims to present this evolutionary relationship based on amino aci...

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Structure of glycerol-3-phosphate dehydrogenase, an essential monotopic membrane enzyme involved in respiration and metabolism.

Sn-glycerol-3-phosphate dehydrogenase (GlpD) is an essential membrane enzyme, functioning at the central junction of respiration, glycolysis, and phospholipid biosynthesis. Its critical role is indicated by the multitiered regulatory mechanisms that stringently controls its expression and function. Once expressed, GlpD activity is regulated through lipid-enzyme interactions in Escherichia coli....

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L-threonine dehydrogenase. Purification and properties of the homogeneous enzyme from Escherichia coli K-12.

L-Threonine dehydrogenase, which catalyzes the conversion of L-threonine to aminoacetone + CO2 presumably via the intermediate formation of alpha-amino-beta-ketobutyrate, has been purified to apparent homogeneity from extracts of a mutant of Escherichia coli K-12 which has constitutively derepressed levels of the enzyme. Three fractionation steps were used including controlled heat denaturation...

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ژورنال

عنوان ژورنال: Acta Crystallographica Section A Foundations of Crystallography

سال: 2008

ISSN: 0108-7673

DOI: 10.1107/s0108767308091952