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Literature DB >> 6462132

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

Abstract

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.

Entities: Chemical Species

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Year: 1981 PMID： 6462132 PMCID： PMC1163386 DOI： 10.1042/bj1990427

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

11 in total

1. Structure and control of phosphofructokinase from Bacillus stearothermophilus.

Authors: P R Evans; P J Hudson
Journal: Nature Date: 1979-06-07 Impact factor: 49.962

Review 2. Phosphofructokinase.

Authors: K Uyeda
Journal: Adv Enzymol Relat Areas Mol Biol Date: 1979

10. Haloacetol phosphates. Potential active-site reagents for aldolase, triose phosphate isomerase, and glycerophosphate dehydrogenase. I. Preparation and properties.

Authors: F C Hartman
Journal: Biochemistry Date: 1970-04-14 Impact factor: 3.162

2 in total

1. pH dependence of the reverse reaction catalyzed by phosphofructokinase I from Escherichia coli: implications for the role of Asp 127.

Authors: I Auzat; J R Garel
Journal: Protein Sci Date: 1992-02 Impact factor: 6.725

2. Expression of rat liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase and its kinase domain in Escherichia coli.

Authors: A Tauler; A J Lange; M R el-Maghrabi; S J Pilkis
Journal: Proc Natl Acad Sci U S A Date: 1989-10 Impact factor: 11.205

2 in total

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

1. Structure and control of phosphofructokinase from Bacillus stearothermophilus.

Review 2. Phosphofructokinase.

3. Rabbit muscle phosphofructokinase. II. Product and dead end inhibition.

4. Studies on the reaction mechanism of skeletal muscle phosphofructokinase.

5. Rabbit muscle phosphofructokinase. The kinetic mechanism of action and the equilibrium constant.

6. Rabbit muscle phosphofructokinase. I. Anomeric specificity; initial velocity kinetics.

7. Rapid labeling of mitochondrial lipids by labeled orthophosphate and adenosine triphosphate.

8. Substrate synergism and phosphoenzyme formation in catalysis by succinyl coenzyme A synthetase.

9. Labeling of the active site of aldolase with glyceraldehyde 3-phosphate and erythrose 4-phosphate.

10. Haloacetol phosphates. Potential active-site reagents for aldolase, triose phosphate isomerase, and glycerophosphate dehydrogenase. I. Preparation and properties.

1. pH dependence of the reverse reaction catalyzed by phosphofructokinase I from Escherichia coli: implications for the role of Asp 127.

2. Expression of rat liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase and its kinase domain in Escherichia coli.