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PMID: 4309306 Published · ppublish English Journal Article

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

The Biochemical journal ·Vol. 114 ·No. 1 ·1969-08-00 ·Pages 19-24

Trentham DR, McMurray CH, Pogson CI

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.

MeSH Terms
Chemical Phenomena Chemistry Fructose-Bisphosphate Aldolase Glyceraldehyde-3-Phosphate Dehydrogenases Glycolysis Hydrogen-Ion Concentration Isomerases Kinetics NAD Phosphoric Acids Spectrum Analysis Trioses
Chemicals
Phosphoric Acids Trioses NAD Glyceraldehyde-3-Phosphate Dehydrogenases Fructose-Bisphosphate Aldolase Isomerases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Trentham D R
McMurray C H
Pogson C I
References (11)
11 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
Published
1969-08-00
Pages
19-24
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1184790
Subset
IM
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