The effect of normal red cell constituents on the activities of red cell enzymes

Satish Srivastava, Ernest Beutler

Research output: Contribution to journalArticle

43 Citations (Scopus)

Abstract

The effect of 2,3-DPG, pyridoxal-5′-P, pyridoxal, pyridoxine creatine and bicarbonate was studied on the activity of red cell glycolytic and pentose phosphate shunt enzymes at saturating and limiting substrate concentrations. 2,3-DPG strongly inhibits the activity of hexokinase, phosphoglucomutase, phosphofructokinase, aldolase and glyceraldehyde phosphate dehydrogenase. In the case of the first four enzymes, 2,3-DPG competes with the substrate and glyceraldehyde phosphate dehydrogenase is inhibited in a noncompetitive fashion. Pyridoxal-5′-P inhibits some of the enzymes inhibited by 2,3-DPG, including hexokinase, phosphoglucomutase, phosphofructokinase and aldolase; in addition, it also inhibits the activity of phosphoglucose isomerase, pyruvate kinase, glucose-6-P dehydrogenase and 6-phosphogluconate dehydrogenase. In some cases, the inhibition was competitive; in others, it was noncompetitive. Creatine and bicarbonate do not significantly inhibit any of the enzymes studied. The studies reported in this report indicate possible roles of 2,3-DPG and pyridoxal-5′-P in the regulation of glucose metabolism in red cells.

Original languageEnglish (US)
Pages (from-to)249-255
Number of pages7
JournalArchives of Biochemistry and Biophysics
Volume148
Issue number1
DOIs
StatePublished - 1972
Externally publishedYes

Fingerprint

2,3-Diphosphoglycerate
Pyridoxal
Cells
Pyridoxal Phosphate
Phosphoglucomutase
Glyceraldehyde
Enzymes
Phosphofructokinases
Oxidoreductases
Fructose-Bisphosphate Aldolase
Hexokinase
Creatine
Phosphates
Bicarbonates
Phosphogluconate Dehydrogenase
Glucose-6-Phosphate Isomerase
Pentoses
Glucose
Pentose Phosphate Pathway
Pyridoxine

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

The effect of normal red cell constituents on the activities of red cell enzymes. / Srivastava, Satish; Beutler, Ernest.

In: Archives of Biochemistry and Biophysics, Vol. 148, No. 1, 1972, p. 249-255.

Research output: Contribution to journalArticle

Srivastava, Satish ; Beutler, Ernest. / The effect of normal red cell constituents on the activities of red cell enzymes. In: Archives of Biochemistry and Biophysics. 1972 ; Vol. 148, No. 1. pp. 249-255.
@article{eadb815468664c629b40696c370aa5ef,
title = "The effect of normal red cell constituents on the activities of red cell enzymes",
abstract = "The effect of 2,3-DPG, pyridoxal-5′-P, pyridoxal, pyridoxine creatine and bicarbonate was studied on the activity of red cell glycolytic and pentose phosphate shunt enzymes at saturating and limiting substrate concentrations. 2,3-DPG strongly inhibits the activity of hexokinase, phosphoglucomutase, phosphofructokinase, aldolase and glyceraldehyde phosphate dehydrogenase. In the case of the first four enzymes, 2,3-DPG competes with the substrate and glyceraldehyde phosphate dehydrogenase is inhibited in a noncompetitive fashion. Pyridoxal-5′-P inhibits some of the enzymes inhibited by 2,3-DPG, including hexokinase, phosphoglucomutase, phosphofructokinase and aldolase; in addition, it also inhibits the activity of phosphoglucose isomerase, pyruvate kinase, glucose-6-P dehydrogenase and 6-phosphogluconate dehydrogenase. In some cases, the inhibition was competitive; in others, it was noncompetitive. Creatine and bicarbonate do not significantly inhibit any of the enzymes studied. The studies reported in this report indicate possible roles of 2,3-DPG and pyridoxal-5′-P in the regulation of glucose metabolism in red cells.",
author = "Satish Srivastava and Ernest Beutler",
year = "1972",
doi = "10.1016/0003-9861(72)90138-5",
language = "English (US)",
volume = "148",
pages = "249--255",
journal = "Archives of Biochemistry and Biophysics",
issn = "0003-9861",
publisher = "Academic Press Inc.",
number = "1",

}

TY - JOUR

T1 - The effect of normal red cell constituents on the activities of red cell enzymes

AU - Srivastava, Satish

AU - Beutler, Ernest

PY - 1972

Y1 - 1972

N2 - The effect of 2,3-DPG, pyridoxal-5′-P, pyridoxal, pyridoxine creatine and bicarbonate was studied on the activity of red cell glycolytic and pentose phosphate shunt enzymes at saturating and limiting substrate concentrations. 2,3-DPG strongly inhibits the activity of hexokinase, phosphoglucomutase, phosphofructokinase, aldolase and glyceraldehyde phosphate dehydrogenase. In the case of the first four enzymes, 2,3-DPG competes with the substrate and glyceraldehyde phosphate dehydrogenase is inhibited in a noncompetitive fashion. Pyridoxal-5′-P inhibits some of the enzymes inhibited by 2,3-DPG, including hexokinase, phosphoglucomutase, phosphofructokinase and aldolase; in addition, it also inhibits the activity of phosphoglucose isomerase, pyruvate kinase, glucose-6-P dehydrogenase and 6-phosphogluconate dehydrogenase. In some cases, the inhibition was competitive; in others, it was noncompetitive. Creatine and bicarbonate do not significantly inhibit any of the enzymes studied. The studies reported in this report indicate possible roles of 2,3-DPG and pyridoxal-5′-P in the regulation of glucose metabolism in red cells.

AB - The effect of 2,3-DPG, pyridoxal-5′-P, pyridoxal, pyridoxine creatine and bicarbonate was studied on the activity of red cell glycolytic and pentose phosphate shunt enzymes at saturating and limiting substrate concentrations. 2,3-DPG strongly inhibits the activity of hexokinase, phosphoglucomutase, phosphofructokinase, aldolase and glyceraldehyde phosphate dehydrogenase. In the case of the first four enzymes, 2,3-DPG competes with the substrate and glyceraldehyde phosphate dehydrogenase is inhibited in a noncompetitive fashion. Pyridoxal-5′-P inhibits some of the enzymes inhibited by 2,3-DPG, including hexokinase, phosphoglucomutase, phosphofructokinase and aldolase; in addition, it also inhibits the activity of phosphoglucose isomerase, pyruvate kinase, glucose-6-P dehydrogenase and 6-phosphogluconate dehydrogenase. In some cases, the inhibition was competitive; in others, it was noncompetitive. Creatine and bicarbonate do not significantly inhibit any of the enzymes studied. The studies reported in this report indicate possible roles of 2,3-DPG and pyridoxal-5′-P in the regulation of glucose metabolism in red cells.

UR - http://www.scopus.com/inward/record.url?scp=0015262292&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0015262292&partnerID=8YFLogxK

U2 - 10.1016/0003-9861(72)90138-5

DO - 10.1016/0003-9861(72)90138-5

M3 - Article

VL - 148

SP - 249

EP - 255

JO - Archives of Biochemistry and Biophysics

JF - Archives of Biochemistry and Biophysics

SN - 0003-9861

IS - 1

ER -