Kinase-catalysed transfer

L-Fucose has been estimated by fucose-kinase-catalysed transfer of [ P]phos-phate from ATP to L-[ H]fucose, followed by electrophoretic separation of the labelled product. ... 

Phosphoroglycerate kinase catalyses the transfer of a phosphoryl residue from 1,3-bisphosphoroglycerate (29), a constituent of the glycolytic pathway, to ADP. It had been postulated that an intermediate in this reaction was a phosphoryl enzyme in which the phosphoryl group was attached to the y-carboxy-group of a glutamyl residue. Recent studies, however, show that the phosphoryl enzyme contains a stoicheiometric amount of (29), and hence is probably a tightly bound (but not covalently linked) complex of the kinase and (29). 

Kinase A type of enzyme that catalyses transfer of phosphate from ATP or GTP... 

Metal cofactors do not always bind to the enzyme but rather bind to the primary substrate. The resulting substrate-metal complex binds to the enzyme and facilitates its activity. Creatine kinase catalyses the transfer of phosphoryl groups from adenosine triphosphate (ATP), which is broken down to adenosine diphosphate (ADP). The reaction requires the presence of magnesium ions. These, however, do not bind to the enzyme but bind to ATP, forming an ATP Mg complex. It is this complex that binds to the enzyme and allows transfer of the phosphoryl group ... 

The generation of NADP is catalysed by NAD kinase, which transfers a phosphate group from ATP onto the 2 -hydroxyl group of the ribose moiety of NAD. A single mammalian NAD kinase has so far been identified NAD kinase activity is essential for cell survival (Agledal et al. 2010). 

Pyruvate kinase catalyses phosphoryl transfer reactions involving ATP. The reaction most important biologically is the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, to form ATP (Scheme 1), although other... 

In other instances there is no evidence of a covalently bonded intermediate. Thus the kinases, which catalyse transfer of a phosphate... 

Enzymes catalysing the transfer of a chemical group, (transfer methyl, acyl, etc.) (EC 2.1 - 2.9) EC2.1 Transf. one-carbon groups (nicotinamide N- Adenylate/creatine kinase/firefly AMP, ADP, ATP ATP Luciferin / Mg21- 19... 

Phosphoryl group transfer reactions add or remove phosphoryl groups to or from cellular metabolites and macromolecules, and play a major role in biochemistry. Phosphoryl transfer is the most common enzymatic function coded by the yeast genome and, in addition to its importance in intermediary metabolism (see Chapter 5), the reaction is catalysed by a large number of central regulatory enzymes that are often part of signalling cascades, such as protein kinases, protein phosphatases, ATPases and GTPases. 

In the preceding sections the conversion of purines and purine nucleosides to purine nucleoside monophosphates has been discussed. The monophosphates of adenosine and guanosine must be converted to their di- and triphosphates for polymerization to RNA, for reduction to 2 -deoxyribonucleoside diphosphates, and for the many other reactions in which they take part. Adenosine triphosphate is produced by oxidative phosphorylation and by transfer of phosphate from 1,3-diphosphoglycerate and phosphopyruvate to adenosine diphosphate. A series of transphosphorylations distributes phosphate from adenosine triphosphate to all of the other nucleotides. Two classes of enzymes, termed nucleoside mono-phosphokinases and nucleoside diphosphokinases, catalyse the formation of the nucleoside di- and triphosphates by the transfer of the terminal phosphoryl group from adenosine triphosphate. Muscle adenylate kinase (myokinase)... 

I n this way we have shown that phosphoryl transfer catalysed by Bacillus stearothermophilus and rabbit skeletal muscle phosphofructokinase (6), and rabbit skeletal muscle pyruvate kinase occurs with inversion of configuration at phosphorus (7). The simplest interpretation of these stereochemical results is that phosphoryl transfer occurs by an in-line mechanism in the enzyme substrate ternary complexes. Stereochemical analysis is thus proving to be of considerable importance for delineating the mechanism adopted by phosphokinases. ... 

T4-DNA kinase. Enzyme isolated from phage T4 infected E. coli which catalyses the transfer of the y-phosphate group of rATP to the 5 -hydroxyl terminus of DNA and RNA T4-DNA ligase. Enzyme isolated from phage T4 infected E. coli which catalyses its formation of a phosphodiester bond between adjacent 5 -phosphorylated and 3 -hydroxy terminated DNA strands... 

The first enzyme in this sequence and the one which is affected by cyclic AMP is a protein kinase. It catalyses the transfer of the terminal phosphate of ATP to phosphorylase b kinase, thereby activating the enzyme. 

Arginine kinase, in the presence of a divalent metal ion, can catalyse the reversible transfer of the terminal phosphoryl residue of ATP to L-arginine. P N.m.r. spectroscopy has recently been used to determine the equilibrium constant for this reaction, and it appears that high enzyme concentrations favour the formation of phosphoroarginine, an observation which may have physiological significance. 

Because of the very high price of ATP, reaction (5.7) must be coupled with a regenerating system, the transfer of phosphate to ADP starting from the enol phosphate of pyruvic acid (an easily accessible and inexpensive phosphate), catalysed by the enzyme pyruvate kinase (reaction (5.8). In the same flask are mixed glucose, phosphoenolpyruvate, hexokinase, pyruvate kinase, and a catalytic quantity of ATP (about 1% mol) and the system produces D-glucose 6-phosphate until the phosphoenolpyruvate runs out. The kinases are easily accessible and, if they are immobilized on an insoluble support (see Section 10.4.1), they are reusable a certain number of times. In this way glucose 6-phosphate can be easily prepared on a 250 g scale (Poliak et al. 1977). 

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