scholarly journals The stereochemical course of phosphoryl transfer catalysed by polynucleotide kinase (bacteriophage-T4-infected Escherichia coli B)

1981 ◽  
Vol 199 (1) ◽  
pp. 273-276 ◽  
Author(s):  
R L Jarvest ◽  
G Lowe
Keyword(s):  
Escherichia Coli ◽  
Phosphorus Atom ◽  
Bacteriophage T4 ◽  
Phosphoryl Group ◽  
Phosphoryl Transfer ◽  
Polynucleotide Kinase ◽  
Gamma S ◽  
Escherichia Coli B

Polynucleotide kinase (bacteriophage-T4-infected Escherichia coli B) catalyses the transfer of the [gamma-16O,17O,18O]phosphoryl group from 5′[gamma(S)-16O,17O,18O]ATP to 3′-AMP with inversion of configuration at the phosphorus atom. The simplest interpretation of this observation is that the [gamma-16O,17O,18O]phosphoryl group is transferred directly from ATP to the co-substrate by an ‘in-line’ mechanism.

scholarly journals The stereochemical course of phosphoryl transfer catalysed by Bacillus stearothermophilus and rabbit skeletal-muscle phosphofructokinase with a chiral [16O,17O,18O]phosphate ester

1981 ◽  
Vol 199 (2) ◽  
pp. 427-432 ◽  
Author(s):  
R L Jarvest ◽  
G Lowe ◽  
B V L Potter
Keyword(s):  
Skeletal Muscle ◽  
Phosphorus Atom ◽  
Bacillus Stearothermophilus ◽  
Ternary Complexes ◽  
Rabbit Skeletal Muscle ◽  
Phosphoryl Group ◽  
Phosphate Ester ◽  
Phosphoryl Transfer ◽  
Enzyme Substrate

Bacillus stearothermophilus and rabbit skeletal-muscle phosphofructokinases catalyse the transfer of the chiral [16O,17O,18O]phosphoryl group from D-fructose 1[(S)-16O,17O,18O],6-bisphosphate to ADP with inversion of configuration at the phosphorus atom. D-Fructose 1[(S)-16O,17O,18O],-bisphosphate was synthesized in situ from sn-glycerol 3[(S)-16O,17O,18O]phosphate. The simplest interpretation of these results is that the phosphoryl group is transferred between substrates in the enzyme substrate ternary complexes by an ‘in-line’ mechanism.

scholarly journals The stereochemical course of yeast hexokinase-catalysed phosphoryl transfer by using adenosine 5′[γ(S)-16O,17O,18O]triphosphate as substrate

1981 ◽  
Vol 199 (1) ◽  
pp. 227-233 ◽  
Author(s):  
G Lowe ◽  
B V L Potter
Keyword(s):  
Ternary Complex ◽  
Phosphoryl Group ◽  
Phosphoryl Transfer ◽  
Enzyme Substrate ◽  
Gamma S ◽  
Yeast Hexokinase

Adenosine 5′[gamma(S)-16O, 17O, 18O]triphosphate has been synthesized and used to determine the stereochemical course of phosphoryl transfer catalysed by yeast hexokinase. The chirality at phosphorus of the D-glucose 6-[16O,17O,18O]phosphate formed was analysed, after cyclization and methylation, by 31P n.m.r. spectroscopy. The phosphoryl transfer was found to occur with inversion of configuration, with a stereoselectivity in excess of 94%. The simplest interpretation of this result is that the phosphoryl group is transferred between substrates in the enzyme-substrate ternary complex by an ‘in line’ mechanism.

scholarly journals The stereochemical course of phosphoryl transfer catalysed by glucokinase.

1982 ◽  
Vol 201 (2) ◽  
pp. 421-423 ◽  
Author(s):  
D Pollard-Knight ◽  
B V L Potter ◽  
P M Cullis ◽  
G Lowe ◽  
A Cornish-Bowden
Keyword(s):  
Rat Liver ◽  
Rate Constants ◽  
Ternary Complex ◽  
The Other ◽  
Chemical Mechanism ◽  
Phosphoryl Group ◽  
Phosphoryl Transfer ◽  
Reaction Proceeds ◽  
Gamma S ◽  
Yeast Hexokinase

Adenosine 5'-[gamma(S)-16O,17O,18O]triphosphate has been used to determine the stereo-chemical course of phosphoryl transfer catalysed by rat liver glucokinase. The chirality of the product, D-glucose 6-[16O,17O,18O]phosphate was analysed by 31P n.m.r. spectroscopy. The reaction proceeds with inversion of configuration at phosphorus. The simplest interpretation of this result, which is the same as that observed with yeast hexokinase [Lowe & Potter (1981) Biochem. J. 199, 277-233], is that the phosphoryl group is transferred between MgATP2- and glucose in the ternary complex by an ‘in-line’ mechanism. It accords with the veiw that the kinetic differences between glucokinase and the other hexokinases arise from differences in rate constants and not from any fundamental differences in chemical mechanism.

Sign in / Sign up

Export Citation Format

Share Document