Literature DB >> 4309306

The active chemical state of D-glyceraldehyde 3-phosphate in its reactions with D-glyceraldehyde 3-phosphate dehydrogenase, aldolase and triose phosphate isomerase.

D R Trentham, C H McMurray, C I Pogson.   

Abstract

Glyceraldehyde 3-phosphate exists as the geminal diol and the free aldehyde in the molar ratio 29:1 in aqueous solution. The rate constant of the conversion of diol into aldehyde is 8.7x10(-2)sec.(-1) in the pH range 7.3-8.6 at 20 degrees . The free aldehyde is the substrate for d-glyceraldehyde 3-phosphate dehydrogenase. Over a wide concentration range of enzyme the rate of conversion of diol into aldehyde is the rate-limiting process in the catalytic oxidation of d-glyceraldehyde 3-phosphate by NAD(+). Aldolase and triose phosphate isomerase both liberate d-glyceraldehyde 3-phosphate as the aldehyde. This suggests that the relatively slow diol-aldehyde interconversion does not restrict the rate of glycolysis.

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Year:  1969        PMID: 4309306      PMCID: PMC1184790          DOI: 10.1042/bj1140019

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


  11 in total

1.  The mechanism of oxidation of aldehydes by glyceralde-hyde-3-phosphate dehydrogenase.

Authors:  E RACKER; I KRIMSKY
Journal:  J Biol Chem       Date:  1952-10       Impact factor: 5.157

2.  Glycolytic control mechanisms. II. Kinetics of intermediate changes during the aerobic-anoxic transition in perfused rat heart.

Authors:  J R Williamson
Journal:  J Biol Chem       Date:  1966-11-10       Impact factor: 5.157

3.  The form of the aldehyde susceptible to enzymic oxidation.

Authors:  J F Naylor; I Fridovich
Journal:  J Biol Chem       Date:  1968-01-25       Impact factor: 5.157

4.  Aspects of the chemistry of D-glyceraldehyde 3-phosphate dehydrogenase.

Authors:  D R Trentham
Journal:  Biochem J       Date:  1968-10       Impact factor: 3.857

5.  Studies on mutarotases. II. Investigations of possible rate-limiting anomerizations in glucose metabolism.

Authors:  J M Bailey; P H Fishman; P G Pentchev
Journal:  J Biol Chem       Date:  1968-09-25       Impact factor: 5.157

6.  The properties and enzymatic significance of the enzyme-diphosphopyridine nucleotide compound of 3-phosphoglyceraldehyde dehydrogenase.

Authors:  B Chance; J H Park
Journal:  J Biol Chem       Date:  1967-11-10       Impact factor: 5.157

7.  Kinetics of triose phosphate isomerase.

Authors:  P M Burton; S G Waley
Journal:  Biochim Biophys Acta       Date:  1968-03-25

8.  Kinetics of malic-lactic transhydrogenase. Effect of the keto-enol tautomerism of oxalacetate on the kinetics of oxalacetate formation and utilization.

Authors:  M I Dolin
Journal:  J Biol Chem       Date:  1968-07-25       Impact factor: 5.157

9.  Isoelectric fractionation, analysis, and characterization of ampholytes in natural pH gradients. IV. Further studies on the resolving power in connection with separation of myoglobins.

Authors:  O Vesterberg; H Svensson
Journal:  Acta Chem Scand       Date:  1966

10.  Enzyme concentrations in tissues.

Authors:  P A Srere
Journal:  Science       Date:  1967-11-17       Impact factor: 47.728

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  30 in total

1.  The existence of an electrophilic component in the reaction catalysed by triose phosphate isomerase.

Authors:  M R Webb; J R Knowles
Journal:  Biochem J       Date:  1974-08       Impact factor: 3.857

2.  Elementary processes of the magnesium ion-dependent adenosine triphosphatase activity of heavy meromyosin. A transient kinetic approach to the study of kinases and adenosine triphosphatases and a colorimetric inorganic phosphate assay in situ.

Authors:  D R Trentham; R G Bardsley; J F Eccleston; A G Weeds
Journal:  Biochem J       Date:  1972-02       Impact factor: 3.857

3.  Studies of triose phosphate isomerase by hydrogen exchange.

Authors:  C A Browne; S G Waley
Journal:  Biochem J       Date:  1974-09       Impact factor: 3.857

4.  Studies on the subunit structure and amino acid sequence of trisoe phosphate isomerase from chicken breast muscle.

Authors:  A J Furth; J D Milman; J D Priddle; R E Offord
Journal:  Biochem J       Date:  1974-04       Impact factor: 3.857

5.  On the possible localization of a gene for triosephosphate isomerase on the short arm of human chromosome 5.

Authors:  F Güttler; E Niebuhr
Journal:  Humangenetik       Date:  1973

6.  pH-dependence of the triose phosphate isomerase reaction.

Authors:  B Plaut; J R Knowles
Journal:  Biochem J       Date:  1972-09       Impact factor: 3.857

7.  L-Glyceraldehude 3-phosphate, a bactericidal agent.

Authors:  C T Tang; R Engel; B E Tropp
Journal:  Antimicrob Agents Chemother       Date:  1977-01       Impact factor: 5.191

8.  The active centre of rabbit muscle triose phosphate isomerase. The site that is labelled by glycidol phosphate.

Authors:  J C Miller; S G Waley
Journal:  Biochem J       Date:  1971-06       Impact factor: 3.857

9.  Studies on human triosephosphate isomerase. 3. Characterization of the enzyme from patients with the cri du chat syndrome.

Authors:  R J Hendrickson; R M Snapka; T H Sawyer; R W Gracy
Journal:  Am J Hum Genet       Date:  1973-07       Impact factor: 11.025

10.  Substrate product equilibrium on a reversible enzyme, triosephosphate isomerase.

Authors:  Sharon Rozovsky; Ann E McDermott
Journal:  Proc Natl Acad Sci U S A       Date:  2007-02-07       Impact factor: 11.205

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