(2R,3R,4R)-2,3,4-三羟基-5-氧代戊基磷酸钡

Meat Science 94(1) , 55-62, (2013)

The formation of ATP breakdown products in chicken M. pectoralis major post-slaughter is reported. The concentrations of metabolites were followed in chicken breast throughout the carcass processing post-slaughter and during chilled storage. The concentration...

Protein J. 31(2) , 137-40, (2012)

Catalytic activity has been demonstrated for holotransketolase in the absence of free bivalent cations in the medium. The two active centers of the enzyme are equivalent in both the catalytic activity and the affinity for the substrates. In the presence of fr...

FEBS Lett. 584(19) , 4169-74, (2010)

Most organisms synthesise the B(6) vitamer pyridoxal 5-phosphate (PLP) via the glutamine amidotransferase PLP synthase, a large enzyme complex of 12 Pdx1 synthase subunits with up to 12 Pdx2 glutaminase subunits attached. Deletion analysis revealed that the C...

Biochemistry 51(9) , 1964-75, (2012)

Prokaryotic phosphopentomutases (PPMs) are di-Mn(2+) enzymes that catalyze the interconversion of α-D-ribose 5-phosphate and α-D-ribose 1-phosphate at an active site located between two independently folded domains. These prokaryotic PPMs belong to the alkali...

Biochemistry 50(51) , 11047-57, (2011)

Spontaneous glycation of bovine heart cytochrome c (cyt c) by the sugar ribose 5-phosphate (R5P) weakens the ability of the heme protein to transfer electrons in the respiratory pathway and to bind to membranes. Trypsin fragmentation studies suggest the prefe...

Biochemistry. (Mosc.) 74(7) , 789-92, (2009)

Catalytic activity of two active sites of transketolase and their affinity towards the substrates (xylulose-5-phosphate and ribose-5-phosphate) has been studied in the presence of Ca2+ and Mg2+. In the presence of Ca2+, the active sites exhibit negative coope...

IUBMB Life 62(11) , 797-802, (2010)

Transketolase (TK, EC 2.2.1.1), the key enzyme of the non-oxidative branch of pentose phosphate pathway of hydrocarbon transformation, plays an important role in a system of substrate rearrangement between pentose shunt and glycolysis, acting as a reversible ...

Biochem. Biophys. Res. Commun. 381(3) , 429-33, (2009)

The 3-keto-L-gulonate 6-phosphate decarboxylase (KGPDC) catalyses the decarboxylation of 3-keto-L-gulonate 6-phosphate to L-xylulose in the presence of magnesium ions. The enzyme is involved in L-ascorbate metabolism and plays an essential role in the pathway...

Biochemistry. (Mosc.) 75(7) , 873-80, (2010)

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 ...

Biochemistry. (Mosc.) 76(9) , 1061-4, (2011)

The Michaelis constant values for substrates of transketolase from human tissues were determined over a wide range of substrate concentrations. It is shown that K(m) values determined by other authors are significantly overestimated and explained why this is ...